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MTAP 1 > Chemistry week 2 > Flashcards

Chemistry week 2 Flashcards

1
Q

Also called Thyroxine-Binding prealbumin or Trashthyretin

A

Prealbumin

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2
Q

Proteins that are not synthesized in the liver

A

Immunoglobulins from activated B cell and Coag factor such as VWF

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3
Q

Transports Vitamin A by binding with the retinal-binding protein

A

Prealbumin

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4
Q

Prealbumin is increased in?

A

Chronic renal failure, Alcoholism, Steroid streatment

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5
Q

Prealbumin is decreased in

A

Malnourished

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6
Q

Most abundant protein in the plasma

A

Albumin

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7
Q

Serves as a mobile respiratory of amino acids for incorporation into other proteins

A

Albumin

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8
Q

Major transport protein

A

Albumin

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9
Q

Negative acute phase reactant

A

Albumin

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10
Q

Good indicator of Cystic Fibrosis

A

Albumin

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11
Q

17 days half-life

A

Albumin

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12
Q

barely 2 days half-life

A

Prealbumin

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13
Q

Important in interpreting calcium and magnesium levels because these ions are bound to these protein.

A

Albumin

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14
Q

Elevation of albumin is seen in?

A

Dehydration
Prolonged application of tourniquet for venipuncture

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15
Q

Presence of this protein is abnormal in urine

A

Albumin

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16
Q

Major component of the a1-globulins

A

Alpha1-antitrypsin

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17
Q

Alpha1-antitrypsin is increased in

A

Inflammation (APR), pregnancy, and contraceptives user

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18
Q

Alpha1-antitrypsin is decreased in

A

Emphysema, Hepatic cirrhosis (juvenile), and other pulmonary disorders

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19
Q

Largest major non-immunoglobulin protein in plasma

A

Alpha 2 - macroglobulin

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20
Q

Rises 10-fold or more in Nephrotic syndrome

A

Alpha 2 - macroglobulin

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21
Q

Alpha 2 - macroglobulin is also increased in

A

Diabetes, and liver disease

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22
Q

Laboratory methods of determination of Alpha 2 - macroglobulin

A

Immunodiffusion (radial type)
Immunonephelometry
ELISA
Latex Agglutination

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23
Q

Forms a complex by binding to prostate specific antigen

A

Alpha 2 - macroglobulin

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24
Q

Associated with Alzheimer’s disease

A

Alpha-1-Antichymotrypsin

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25
Q

Serine proteinase with Cathepsin G

A

Alpha-1-Antichymotrypsin

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26
Q

Binds and inactivate PSA

A

Alpha-1-Antichymotrypsin

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27
Q

Alpha-1-Antichymotrypsin is increased in

A

infection, malignancy, burns, Myocardial infarction

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28
Q

Alpha-1-Antichymotrypsin is decreased in

A

Liver disease

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29
Q

Marker of kidney function specifically the tubular function

A

β-2 Microglobulin

because it can readily pass to the glomerulus but it is reabsorbed by the tubule

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30
Q

Light chain component of the major histocompatibility complex (HLA)

A

β-2 Microglobulin

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31
Q

Responsible for causing Dialysis-associated amyloidosis

A

β-2 Microglobulin

kasi it forms a beta plated sheath kaya nag foform siya ng formation ng amyloid

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32
Q

β-2 Microglobulin is increased in

A

Renal failure, Multiple myeloma, HIV, and inflammatory disease such as RA and SLE

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33
Q

Method of determination for β-2 Microglobulin

A

Immunoassay

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34
Q

Carrier of hemoglobin and an APR

A

Haptoglobin

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35
Q

Major protein migrating in the alpha-2 region

A

Haptoglobin

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36
Q

Combines with hemoglobin released by lysed red cells in order to preserve body iron and protein stores

A

Haptoglobin

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37
Q

Haptoglobin is increased in

A

Stress, Infection, myoglobinuria, inflammation, and tissue necrosis

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38
Q

Haptoglobin is decreased in

A

Intravascular hemolysis, and hemoglobinuria

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39
Q

Also known as siderophilin

A

Transferrin

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40
Q

Major beta globulin transport protein for ferric ions

A

Transferrin

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41
Q

Great impact in hemoglobin production

A

Transferrin

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42
Q

Low of this protein causes anemia

A

Transferrin

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43
Q

Transferrin is increased in

A

pregnant women, IDA, Hemochromatosis

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44
Q

Transferrin is decreased in

A

Liver disease, Nephrotic syndrome, and malnutrition

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45
Q

Most abundant of the coag factor

A

Fibrinogen

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46
Q

Marker for CVD

A

Fibrinogen

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47
Q

Fibrinogen is increased in

A

Inflammation, elevated with other APR, pregnancy, and the use of contraceptive

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48
Q

Fibrinogen is decrease in

A

Extensive coagulation kasi niuuse up niya yung fibrinogen

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49
Q

Marker for wilson’s disease

A

Ceruloplasmin

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50
Q

Copper binding protein for target tissues and organs

A

Ceruloplasmin

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51
Q

Responsible in oxidizing iron from ferrous to ferric through the ferroxidase enzyme

A

Ceruloplasmin

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52
Q

Kayser-Fleishcer ring in the cornea

A

Copper toxicity

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53
Q

Menke’s disease that causes curly hair called kinky-hair syndrome and skin is ligher

A

Copper deficiency

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54
Q

Ceruloplasmin is increased in

A

Inflammation, Cancer, Pregnancy

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55
Q

Ceruloplasmin is decreased in

A

Wilson’s disease, Malnutrition, Malabsorption, Nephrotic conditions, and Menke’s disease

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56
Q

Binds heme released by degradation of hemoglobin

A

Hemopexin

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57
Q

Early marker of hemolytic condition

A

Hemopexin

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58
Q

Profoundly decreased in intravascular hemolysis

A

Hemopexin

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59
Q

Also known as orosomucoid

A

α1-Acid Glycoprotein

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60
Q

Binds to progesterone and could be important in its transport or metabolism

A

α1-Acid Glycoprotein

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61
Q

Binds to quinidine

A

α1-Acid Glycoprotein

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62
Q

Can be used in bacterial infection in neonatal population

A

α1-Acid Glycoprotein

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63
Q

α1-Acid Glycoprotein is increased in

A

Pregnancy, Cancer (neoplasia), other increased cell proliferation condition, Rheumatoid arthritis, Pneumonia

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64
Q

Contains carbohydrate molecule and sialic acid

A

α1-Acid Glycoprotein

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65
Q

Major acute phase reactant

A

C-Reactive Protein

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66
Q

Marker for CVD

A

C-Reactive Protein

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67
Q

Binds with C-polysaccharide of the pneumococcal bacteria and precipitate with the C substance

A

C-Reactive Protein

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68
Q

General scavenger molecule

A

C-Reactive Protein

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69
Q

CRP is ____ in bacterial infection and ____ in viral infection

A

High, Low

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70
Q

C-Reactive Protein is increased in

A

pneumococcal infections, Rheumatic fever, MI, Gout, RA

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71
Q

Derived from the fetal yolk sac and most abundant protein in the fetal serum

A

Alpha-I-Fetoprotein (AFP)

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72
Q

Alpha-I-Fetoprotein (AFP) is increase at what week of gestation?

A

13th week

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73
Q

Alpha-I-Fetoprotein (AFP) peaks at ___ month

A

7-8 months

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74
Q

AFP in adult means

A

Liver carcinoma

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75
Q

Alpha-I-Fetoprotein (AFP) is increased in

A

Amniotic fluid and serum in neural tube defect (spina bifida)

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76
Q

Alpha-I-Fetoprotein (AFP) is decreased in

A

Down’s syndrome

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77
Q

used as gold markers for myocardial
infarction since it increases during heart attack

A

Troponin I and T

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78
Q

Inhibitory subunit of troponin

A

Troponin I

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79
Q

Tropomyosin-binding subunit of troponin

A

Troponin T

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80
Q

Calcium-binding subunit of troponin

A

Troponin C

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81
Q

established firmly as the gold standard in the diagnosis of myocardial damage

A

Cardian troponin (cTN )

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82
Q

Most abundant troponin subunit

A

Troponin C

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83
Q

Marker for congestive heart failure

A

BNP and NTBNP

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84
Q

Released by the Myocardium of the Heart that regulates sodium
from cardiac muscles

A

BNP and N-Terminal-BNP

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85
Q

Induces natriuresis which affects the excretion of sodium through the kidney or renal excretion

A

BNP and N-Terminal-BNP

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86
Q

Marker for possible premature delivery

A

Fibronectin

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87
Q

Marker of HAVING cardiovascular diseases

A

Adiponectin

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88
Q

Lower levels of adiponectin correlate with an increased risk of?

A

Heart disease , type 2 DM, and metabolic syndrome, and obesity

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89
Q

Marker of renal function

A

Beta trace protein

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90
Q

Marker of CSF leakage

A

Beta trace protein

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91
Q

Diagnosis of perilymphatic fluid distulas

A

Beta trace protein

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92
Q

Marker for the early assessment of changes to GFR

A

Cystatin C

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93
Q

Cystatin C is increased in

A

Renal disease, Liver disease, Obesity, muscular diseases

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94
Q

Used to differentiate which type of condition is causing the increase of Creatinine.

A

Cystatin C

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95
Q

Considered as a nephrotoxin

A

Myoglobin

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96
Q

2% of total muscle protein

A

Myoglobin

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97
Q

Early marker of cardiac condition. Immediately increases in case of MI but not specificity

A

Myoglobin

pero not specific kasi pwede siya manggaling sa skeletal muscles

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98
Q

Myoglobin is increased in

A

MI, chest pain, skeletal disorders, Rhabdomyolysis, Strenuous exercise, IM injection, Myoglobinuria

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99
Q

Protein polysaccharide complex produced and deposited in tissue during some chronic infections, malignancies, and rheumatologic disorders

A

Amyloid

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100
Q

Amyloid is readily stained by

A

Congo red

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101
Q

o Digestion of protein; Measurement of Nitrogen Content
o Reference method; Assume average nitrogen content of 16%

A

Kjedahl

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102
Q

o Measurement of refractive index due to solutes in serum
o Rapid and Simple; Assume nonprotein solids are present in
same concentration as in the calibrating serum

A

Refractometry

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103
Q

o Formation of Violet-colored chelate between Cu2+ ions and
peptide bonds
o Routine Method; Requires at least two peptide bonds and an
alkaline medium

A

Biuret

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104
Q

o Protein binds to dye and causes a spectral shift in the
absorbance maximum of the dye
o For Research Use

A

Dye binding

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105
Q

o Globulins are precipitated in high salt concentrations; Albumin
in supernatant is quantitated by biuret reaction
o Labor Intensive

A

Sal precipitation

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106
Q

o Albumin binds to dye; causes shift in absorption maximum
o Organic and Nonspecific for albumin

A

Methyl orange

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107
Q

o Albumin binds to dye; causes shift in absorption maximum
o Many interferences (salicylates, bilirubin)

A

HABA (2,4’-Hydrixyazobenzene-Benzoic Acid)

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108
Q

o Albumin binds to dye; causes shift in absorption maximum
o Sensitive; Overestimates low albumin levels
o Most commonly used dye

A

BCG (Bromcresol Green)

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109
Q

o Albumin binds to dye; causes shift in absorption maximum
o Specific, Sensitive, Precise

A

BCP (Bromcresol Purple)

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110
Q

o Proteins separated based on electric charge
o Accurate; Gives overview of relative changes in different protein
fractions

A

Electrophoresis

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111
Q

A-1 globulin’s specific proteins

A

α-1-antitrypsin, α-acid glycoprotein

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112
Q

α-2-Globulin’s specific protein

A

Ceruloplasmin, haptoglobin, α-2-microglobulin

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113
Q

β-Globulin’s specific protein

A

LDL, VLDL, Transferrin, Hemopexin, Complement,
Fibrinogen

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114
Q

γ-Globulin’s specific protein

A

Immunoglobulin

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115
Q

Electrophoresis pattern

A

Prealbumin > Albumin > A1 globulin > a2 globulin > b globulin > gamma globulin

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116
Q

Monoclonal peak in gamma-globulin region which is a marker of multiple myeloma

A

Bence-jones protein

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117
Q

Tall spike pattern which shows only one variation of protein

A

Monoclonal peak

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118
Q

Tall and curve pattern which shows many variation of proteins are high

A

Polyclonal peak

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119
Q

Polyclonal peak is typically seen in

A

Infections

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119
Q

Nephrotic syndrome electrophoretic pattern

A

Increase alpha 2 macroglobulin

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119
Q

Agammaglobulinemia

A

Depleted or absence immunoglobulin in immunosuppressed patients

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120
Q

Globulins are precipitated using Sodium Sulfate, Sodium Sulfite,
Ammonium Sulfate, or Methanol leaving albumin in solution

A

precipitation

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121
Q

Order of protein elution is by molecular weight or size from largest first to smallest last

A

Gel filtration

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122
Q

Based on the charge of proteins which bind to heads of a charged support medium

A

Ion exchange chromatography

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123
Q

Samples are applied at high salt and eluted with low salt

A

Hydrophobic chromatography

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124
Q

Based on specific binding between a protein of interest and another protein that has been covalently linked to the solid medium of a column

A

Affinity chromatography

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125
Q

Separation method based on flow through a capillary tube that can be tailored to resolution of different molecules based on size, hydrophobicity, or stereospecificity

A

Capillary electrophoresis

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126
Q

Reference method of protein detection and quantitation

A

Kjeldahl technique

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127
Q

The ammonium can then be quantitated by conversion to ammonia gas and titration as a base or be nesslerization

A

Kjeldahl technique

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128
Q

Total serum protein is obtained by multiplying the value of TPN by?

A

6.25

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129
Q

Nessler reagent contains?

A

Double iodide of potassium and mercury to form a mercuric ammonium iodide which is YELLOW in color

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130
Q

Accurate for measure serum protein concentration as dissolved solute for levels above 2.5 g/dL

A

Refractive index

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131
Q

Cannot be used for urine protein measurements because of excess amounts of solutes in relation to the protein

A

Refractive index

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132
Q

Used widely as a screening test for Hemoglobin concentration in whole blood

A

Specific Gravity

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133
Q

Used to measure protein concentration in CSF or urine

A

Turbidimetric method

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134
Q

Turbidimetric method reference ranges
Negative

A

Clear sample. No turbidity
<20mg/dL

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135
Q

Turbidimetric method reference ranges
Trace

A

Very faint precipitate
20-200 mg/dL

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136
Q

Turbidimetric method reference ranges
1+

A

Small degree turbidity
100-1000 mg/dL

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137
Q

Turbidimetric method reference ranges
2+

A

Moderate turbidity
1000-2500 mg/dL

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138
Q

Turbidimetric method reference ranges
3+

A

Heavy turbidity
2500-4500 mg/dL

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139
Q

Turbidimetric method reference ranges
4+

A

Heavy flocculation/Clumping
>4500 mg /dL

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140
Q

Measure peptide linkage or peptide bond

A

Biuret method

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141
Q

Reagents are copper sulfate, Tartrate salt, Potassium Iodide

A

Biuret method

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142
Q

Presence of two or more peptide bonds in which form purple complex with copper, salts in alkaline solution

A

Biuret method

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143
Q

Involves oxidation of phenolic compounds such as tyrosine, tryptophan, and histidine to give a deep blue color

A

Folin-Ciocaltou reagent

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144
Q

Used for CSF proteins because they have less than 1% protein

A

Coomasie brillant dye

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145
Q

Produces a violet color by reacting with primary AMINES

A

Ninhydrine

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146
Q

Total protein =

A

Albumin + Globulins

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147
Q

Total protein reference range

A

6.5-8.5 g/dL

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148
Q

Total protein is ____ in these circumstances
o Dehydration
o Severe Exercise
o Infection
o Cancer

A

Increased

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149
Q

Total protein is ____ in these circumstances
o GI Cancers
o Liver Disease
o Malnutrition
o Low Thiamine
o Glomerulonephritis

A

Decreased

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150
Q

Albumin reference range

A

3.5-5.0 g/dL

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151
Q

Albumin is ______ in these circumstances
o Dehydration
o Sunstroke
o Exercise
o Multiple Sclerosis
o Hypothyroidism

A

Increased

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152
Q

Albumin is ______ in these circumstances
o Pregnancy
o Malnutrition
o Malabsorption
o Liver disease
o Kidney disease
o Burns

A

Decreased

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153
Q
  • Rare inherited disorders of amino acid metabolism
  • Causes deficiency, specifically enzymes
A

Aminoacidopathies

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154
Q
  • Most common aminoacidopathy that is tested in newborn screening
  • Autosomal recessive trait and occurs approximately in 1/15,000 births
  • Absence of PAH (Phenylalanine-4-Monooxygenase) which catalyzes
    the conversion of phenylalanine to tyrosine
A

Phenylketonuria

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155
Q

Reference method of phenylketonuria

A

High performance liquid chromatograph

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156
Q

Used for inhibition with B2-thienylalanine in phenylketonuria

A

Bacillus subtilis

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157
Q
  • Characterized by excretion of tyrosine catabolites in urine
  • Defects in fumarylacetoacetase
  • Causes accumulation of Tyrosine crystals in the urine which are
    needle-shaped urine crystals
A

Tyrosinemia

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158
Q

Laboratory test for Tyrosinemia

A

Ion-exchange column chromatography

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159
Q
  • Deficiency of homogentisate oxidase in tyrosine catabolic pathway
  • Build up of homogentisic acid
    o Effect: Homogentisic acid accumulates in connective tissue causing generalized pigmentation and arthritis-like degeneration. Homogentisic acid causes to darken upon
    exposure to air.
A

Alkaptonuria

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160
Q

Laboratory test for alkaptonuria

A

Blue color when ferric chloride is added to urine

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161
Q
  • Deficiency of branched chain keto-acid decarboxylase
  • Build up of leucine, isoleucine, and valine
    o Effects: Mental retardation, convulsion, acidosis, hypoglycemia,
    and death. Burnt-sugar odor of urine, breathe, and skin
A

Maple syrup urine disease

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162
Q

Screening test for MSUD

A

Modified Guthrie test that detects elevated plasma leucine

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163
Q

Uses as antagonist for the bacteria in MSUD

A

4-azaleucine

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164
Q
  • Impaired activity of the enzyme Cystathionine β-Synthase
  • Results in elevated plasma and urine levels of the precursors
    homocysteine and methionine
    o Effects: Late Childhood – thrombosis, osteoporosis, dislocated
    lenses
A

Hemocystinuria

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165
Q

Neonatal screening test for hemocystinuria

A

Guthrie test using L-methionine sulfoximine

166
Q

Confirmatory test for hemocystinuria

A

High performance liquid chromatography >2mg/dL

167
Q

Lab test for Isovaleric acidemia

A

Chromatography, Mass spectrometry

168
Q

Lab test for cystinuria

A

Test urine cyanide-nitroprusside (+) red color to purple

169
Q

Marker for arginosuccinic aciduria and citrullinemia

A

Citrulline

170
Q

Lab test for arginosuccinic aciduria and citrullinemia

A

Mass spectrometry

171
Q

Urea in plasma

A

45-50%

172
Q

Urea in urine

A

86%

173
Q

Amino acids in plasma

A

25%

174
Q

Uric acid in plasma

A

10%

175
Q

Uric acid in urine

A

1.7%

176
Q

Creatinine in plasma

A

5%

177
Q

Creatinine in urine

A

4.5%

178
Q

Creatine in plasma

A

1-2%

179
Q

Ammonia in plasma

A

0.2%

180
Q

Ammonia in urine

A

2.8%

181
Q

Removal of the substance from plasma into the urine

A

Clearance test

182
Q

Plasma concentration and clearance is

A

Inversely proportional

183
Q

Gold standard and reference method for GFR clearance test

A

Inulin clearance

184
Q

Excellent measure of renal function since this is freely filtered by glomeruli but not reabsorbed

A

Creatinine clearance test

185
Q

Waste product of muscle metabolism

A

Creatinine

186
Q

Creatinine is directly proportional to?

A

Muscle Mass

187
Q

Denotes damage of the PCT because it is reabsorbed by the PCT

A

Cystatin C

188
Q

Earliest GFR test

A

Urea clearance

189
Q

Not affected by muscle mass, age, and gender

A

Cystatin C

190
Q

First metabolite to elevate in kidney disease

A

BUN

191
Q

Major NPN

A

Urea

192
Q

45% of total NPN

A

BUN

193
Q

Urea formula

A

BUN x 2.14

194
Q

Methods of determination of BUN

A

Chemical method = Fearon’s reaction/Diacetyl monoxime
Enzymatic method = Uses urease

195
Q

Fearon’s reaction end color

A

Yellow

196
Q

Reference method for ALL NPN

A

Isotope Dilution mass spectrometry (IDMS)

197
Q

End product of muscle metabolism

A

Creatinine

198
Q

Index of overall renal function

A

Creatinine

199
Q

Creatinine is composed of? (GAM)

A

Glycine, Arginine, Methionine

200
Q

Method of determination of creatinine

A

Chemical method = Jaffe reaction

201
Q

Jaffe reaction end color

A

Orange-red color

202
Q

Marked elevation of plasma urea and other NPNs accompanied by acidemia and hyperkalemia

A

Uremia

203
Q

PBS = (+) burr cells

A

Uremia

204
Q

Very high plasma urea concentration accompanied by renal failure

A

Uremia

205
Q

Elevations of concentration of nitrogenous substances such as urea and creatinine in the blood

A

Azotemia

206
Q

Reduced renal blood flow
Increased creatinine and urea that is before kidneys
Problem in systemic circulation problem

A

Prerenal azotemia

207
Q

Very high plasma urea concentration accompanied by renal failure

A

Renal azotemia

208
Q

Caused by obstruction anywhere in the urinary tract

A

Postrenal azotemia

209
Q

Major end product of purine (adenine and guanin) metabolism

A

Uric Acid

210
Q

Method of determination for BUA

A

Chemical method = Caraway method
Enzymatic method = uricase (most common)

211
Q

Reagent in caraway method

A

Phosphotungstic acid

212
Q

End color of caraway method

A

(+) Blue

213
Q

Uric acid is increased in

A

Gout
Lesch-nyhan syndrome (Hypoxanthine guanin phosphotibosyltransferase deficiency)
Chronic renal disease

214
Q

Uric acid is decreased in (OLD)

A

Liver disease
Overtreatment with allopurinol
Defective tubular reabsorption - eg. Fanconi syndrome (defective PVT reabsorptiom)

215
Q

Striking proteinuria
Decreased serum albumin and total protein
Relative increased in alpha 2 macroglobulin and beta-globulin fractions
Increases in serum creatinine, BUN, and Uric acid

A

Nephrotic syndrome

216
Q

Alpha2- globulin band spike

A

Nephrotic syndrome

217
Q

Beta gamma bridging

A

Hepatic cirrhosis

218
Q

Alpha1-globulin flat curve

A

Juvenile cirrhosis

219
Q

Lipiduria is present in

A

Nephrotic syndrome (cholesterol crystals, oval fat bodies, waxy casts may be present)

220
Q

Elevated urine protein
Increased BUN and CREATININE (2)
Red cells and red cell casts in urine

A

Glomerulonephritis

221
Q

Oliguria
increase in BUN and creatinine
Electrolyte and acid/base alteration

A

Renal failure

222
Q

Specific alteration in excretion of amino acids, electrolytes, or other specific biochemicals

A

Tubular defects

223
Q

Acute kidney injury biochemical changes: INC OR DEC
Calcium, Bicarbonate, Sodium

A

Decreased (CABISO)

224
Q

Acute kidney injury biochemical changes: INC OR DEC
Urea, creatinine, potassium, phosphate, magnesium, hydrogen ion

A

Increased

225
Q

Early biomarker for diagnosis acute kidney injury

A

Neutrophil gelatinase associated Lipocalin
pag walang NGAL = Cystatin C

226
Q

Produced from the deamination of amino acids during protein metabolism

A

Ammonia

227
Q

Removed from the circulation and converted urea in the liver

A

Ammonia

228
Q

Methods of determination of ammonia

A

Berthelot reaction
Nesslerization reaction
Enzymatic

229
Q

End color of Berthelot reaction

A

Blue

230
Q

Enzymatic method of determination of ammonia uses?

A

Glutamate dehydrogenase

Enzymatic method is the most common method

231
Q

Ammonia is increased in

A

Hepatic failure, Reye’s syndrome, inherited deficiencies of urea cycle enzymes

232
Q

NPN from highest to lowest UA-UC-CA

A

Urea > Amino acid > Uric acid > Creatinine > creatine > ammonia

233
Q

Major end product of protein metabolism

A

Urea

234
Q

Oldest method that uses less than 1mL of serum sample to measure urea through nitrogen concentration
N → NH4 + alk. K2HgI4 → NH2HgI3

A

Micro-kjedahl nessler

235
Q
  • Urease catalyzes the breakdown of urea into separate carbon dioxide
    and ammonium ion that is usually collected from Jack Beans
    o Urea → CO2 + NH3
    o NH3 + Nessler’s Reagent → NH2HgI3
A

Urease-nessler method

236
Q

Normal value of urea

A

7-18 mg/dL
2.5-6.4 mmol/L

237
Q

Conversion factor for urea

A

0.357

237
Q

Ratio of BUN to creatinine

A

10-20:1

237
Q
  • Available on Ektachem analyzer wherein creatinine is hydrolyzed to N-methyldantolin and ammonia by creatinase. The ammonia is then
    made to react with alpha-ketoglutarate and NADH in the presence of
    glutamate dehydrogenase forming glutamate and NAD. The decrease
    in NADH is measured fluorometrically.
  • Measures the oxidation of NADH into NAD at 340 nm
A

Creatinase method

238
Q
  • Creatinine is hydrolyzed to creatine by creatinine aminohydrolase
    followed by a series of coupled enzyme reactions in which creatine
    reacts with creatinine kinase, pyruvate kinase, and lactate
    dehydrogenase, culminating in the oxidation of the NADH.
  • Pyruvate + NADH → Lactate Dehydrogenase → Lactate + NAD
  • Measure the oxidation at 340 nm
  • Alternatives:
    o Trinder’s Reaction can also be used where product is hydrogen
    peroxide (H2O2)
    ▪ Sarcosine reacts to Creatinine which also produce
    hydrogen peroxide (H2O2)
A

Creatinine aminohydrolase

239
Q

Normal value of creatinine

A

0.6-1.2 mg/dL
53-106 umol/L

  • Jaffe Method:
    o Male: 0.9–1.3 mg/dL (80–115 µmol/L)
    o Female: 0.6–1.1 mg/dL (53–97 µmol/L)
  • Enzymatic Method:
    o Male: 0.6–1.1 mg/dL (53–97 µmol/L)
    o Female: 0.5–0.8 mg/dL (44–71 µmol/L
240
Q

Conversion factor for creatinine

A

88.4

241
Q

End product of nucleic acid metabolism

A

BUA

242
Q

How many % of the filtered uric acid is reabsorbed?

A

89%

243
Q

Modification of caraway’s method
UA + PTA → tungsten blue
Uses Na2CO3 (Sodium Carbonate) as color stabilizer

A

Henry’s method

244
Q

Addition if this will increase BUA’s stability to bacterial destruction

A

Thymol

245
Q

Anticoagulant than cannot be used in BUA determination

A

potassium oxalate

246
Q

Normal values for BUA

A

o Men – 4.0 - 8.5 mg/dL (0.25 - 0.50 mmol/L)
o Women – 2.7 - 7.3 mg/dl (0.16 - 0.43 mmol/L)

247
Q

Conversion factor for BUA

A

0.0595

248
Q

BUA is _____ in these circumstances:
Von Gierke’s disease
Lactic acidosis
Toxemia of pregnancy

A

Increased

249
Q

BUA is _____ in these circumstances:
Fanconi’s syndrome
Wilson’s disease
Hodgkin’s disease

A

Decreased

250
Q

Carry blood towards glomerulus

A

Afferent arterioles

251
Q

Carry blood away from glomerulus

A

Efferent arterioles

252
Q

Collect the filtrate

A

Bowman’s capsule

253
Q

o Regulates the reabsorption and excretion of Sodium
o Produced by the adrenal cortex; influence of the renin–
angiotensin mechanism (RAAS)
o Triggered by decreased blood flow or blood pressure in the
afferent renal arteriole
o Decreased plasma sodium
o Stimulates sodium reabsorption in the distal tubules and
potassium and hydrogen ion secretion
o When absorbing sodium, water is also reabsorbed in exchange
for potassium and hydrogen molecules which are excreted.

A

Aldosterone

254
Q

o Arginine Vasopressin
o Regulates the excretion of water
o Peptide hormone secreted by the posterior pituitary
o Response to increased blood osmolality
o Released when blood volume decreases by more than 5%–10%
o Stimulates water reabsorption
o Water diffuses passively from the lumen of the tubules resulting
in more concentrated urine and decreased plasma osmolality

A

ADH

255
Q

measures the plasma flow in the kidney

A

Para-amino hippurate test (PAH) or Diodrast Test

256
Q

measures of the excretion of dye which is directly proportional to the renal mass to determine the renal blood flow

A

Phenosufophthalein (PSP) dye excretion test

257
Q

measures the renal concentrating capability
of the kidney using the ff:
▪ Reagent Strip
▪ Urinometer

A

SG

258
Q

Measure the balance between solutes and solvent

A

Osmolality

259
Q

Osmolality formula

A

1.86 x Sodium + (Glucose/18) + (BUN/2.8)

260
Q

Measures and determine the capability of the kidney to balance out, concentrate, and filter out the solutes coming from the renal blood flow

A

Fishberg concentration test

261
Q

Considered as biochemical catalysts (speed up chemical reactions)

A

Enzymes

262
Q

Site where substrates attached and undergo chemical reaction

A

Active site

263
Q

Site opposite to the active site where regulator molecules attached (inhibitory)

A

Allosteric site

264
Q

Nonprotein molecules that maybe necessary for enzyme activity

A

Cofactors

265
Q

Inorganic cofactor (does not have carbon)

A

Activator

266
Q

Organic cofactor

A

Coenzyme

267
Q

Coenzyme that is bound tightly to the enzyme is called?

A

Prosthetic group

268
Q

Enzymes existing in different forms within the same individual

A

Isoenzyme

269
Q

Forms a complete and active system
Compose of apoenzyme (enzyme itself) and coenzyme

A

Holoenzyme

270
Q

Enzymes that are originally secreted from the organ of production in a structurally inactive form

A

Zymogens and proenzymes

271
Q

High specific: Acid phosphatase (ACP)

A

Rbcs, prostate gland

272
Q

High specific: Alanine aminotransferase

A

Liver

273
Q

High specific: Amylase

A

Pancreas, salivary glands

274
Q

High specific: Lipase

A

Pancreas

275
Q

Moderate specific: Aspartate aminotransferase (AST)

A

Liver, heart, skeletal muscle

276
Q

Moderate specific: Creatine kinase

A

Heart, Skeletal muscle, Brain

277
Q

Low specificity: Alkaline phosphatase (ALP)

A

Liver, bone, kidney, Placenta, Intestine

278
Q

Low specificity: Lactate dehydrogenase

A

All tissues

279
Q

Least specific enzyme

A

LDH

280
Q

Catalyzes an oxidation-reduction reaction between two substrate

Uses dehydrogenase as the suffix

A

Oxidoreductase

281
Q

Catalyze the transfer of a group other than hydrogen from one substrate to another

Uses transferase and kinase

A

Transferase

282
Q

Catalyzes hydrolysis of various bonds

Suffix ase and in

A

Hydrolase

283
Q

Catalyzes the removal of substrates WITHOUT hydrolysis

Contains double bonds

A

Lyase

284
Q

Catalyze the interconversion of geometric, optical, or positional isomers

suffix isomerase

A

Isomerase

285
Q

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bond in ATP

suffix -synthase

A

Ligases

286
Q

First order kinetics:
Reaction rate is __________ to substrate concentration

A

Directly proportional

287
Q

Zero order kinetics:
Reaction rate depends only on _______________

A

enzyme concentration

288
Q

The __________ the enzyme level, the faster the reaction will proceed because ____ enzymes are present to bind with the substrate

A

Higher, more

289
Q

pH of enzyme

A

7.0 - 8.0

290
Q

Increasing the temperature will ____ the rate of chemical reaction

A

Increase

291
Q

For each ___ degree increase in temperature, the rate of the reaction will approx. double

A

10 degree

292
Q

Physically bind to the active site of an enzyme and compete with the substrate for active site
Reversible because enzymes is not damaged

A

Competitive inhibitors

293
Q

Bind an enzyme at a place other than the active (allosteric site) and may be reversible or irreversible

A

Noncompetitive inhibitors

294
Q

Is another kind of inhibition in which inhibitor binds to the Enzyme -substrate complex

A

Uncompetitive inhibitors

295
Q

Has the capability to bind either on the enzyme or the enzyme-substrate complex at their active sites

It would not wait for a substrate to bind with enzyme

A

Mixed inhibitor

296
Q

Optimal temperature for enzymes

A

37C

297
Q

Increased temp for enzymes

A

40-50C

298
Q

Temp of denaturation

A

56C

299
Q

Stop reaction temperature

A

-20C

300
Q

Phenomenon that states that a certain enzyme has the ability to adapt to their biochemical systems

A

Enzyme induction

301
Q

Reaction that is initiated by addition of substrate
Reaction is allowed to proceed for a period of time
Measurement is done at the END of the reaction

A

Endpoint analysis / Fixed time analysis

302
Q

Change in concentration of the indicator substance at several intervals

Continuous measurement of change in concentration as function of time

A

Multi-point and Kinetic assay/ Continuous monitoring

303
Q

Units used to denote/express enzyme activity

A

IU and KATAL

304
Q

Conventional unit

A

IU/L

305
Q

Equivalent to the amount of enzyme that has catalyzes the conversion of 1 MICROMOLE of substrate per MINUTE under controlled condition

A

IU/L

306
Q

System internationale unit

A

Katal unit

307
Q

Equivalent to the amount of enzyme that has catalyzes the conversion of 1 MOLE of substrate per SECOND under controlled conditions

A

Mol/s

308
Q

Enzymes that has already undergone post translational mutations

A

Isoforms

309
Q

Enzymes whose metal ions are intrinsically part of the molecule

A

Metalloenzyme

310
Q

Defines the class to which the enzyme belongs

A

First number

311
Q

Indicates subclass and sub class to which the enzyme is assigned

A

Two middle numbers

312
Q

A specific serial number to which the enzyme is assigned

A

Last number

313
Q
  • Gives the means to determine total enzyme concentration in serum
    and other body fluids
  • Accurately describes virtually all single-substrate enzyme-catalyzed
    reactions and many bisubstrate reactions in which the concentration
    of one substrate is constant throughout the course of the reaction.
A

Michaelis-Menten equation

314
Q

Another means of showing how the speed of the reaction occurs based
on the given Michaelis-Menten Constant, Maximum Velocity, and
Substrate Concentration

A

LINEWEAVER-BURKPLOT EQUATION

315
Q

Enzymes combine with only one substrate and catalyzes only one corresponding reaction

A

Absolute specificity

316
Q

Enzymes combining with all substrates containing a particular chemical group

A

Group specificity

317
Q

Enzymes are specific to chemical bonds

A

Bond specificity

318
Q

Enzymes that predominantly combine with one optical isomer of a certain compound

A

Stereoisomeric specificity

319
Q

Based on the rigid enzyme molecule which the substrate fit

A

Emils Fisher’s Lock and Key theory

320
Q

Based on the attachment of a substrate to the active site of an enzyme, which then causes conformational changes in the enzyme.

More acceptable theory because the protein molecule is flexible enough to allow changes

A

Koshland’s induced fit theory

321
Q

Enzymes are stable at ____ for at least 24 hours`

A

6C

322
Q

Involved in the reversible phosphorylation of creatine by ATP

A

Creatine Kinase

323
Q

Predominant physiologic function occurs in muscle cells, where it is involved in the storage of high-energy creatine phosphate

A

Creatine Kinase

324
Q

Heart specific creatine kinase

A

CK-MB

325
Q

Reference value of creatine kinase

A
  • Male: 15-160 U/L
  • Female: 15-130 U/L
    o CK-MB: 6% of total CK
326
Q

Electrophoresis pattern of Creatine kinase

A

CK-BB - Most rapidly moving isoenzyme which is a product of chromosome 14 (anodal)
CK-MB - Hybrid which is from chromosome 19
CK-MM - slowest and most common form (most cathodal, least anodal)

327
Q

is the first enzyme to increase
after onset signs and symptoms after 4-6 hours (Peaks at 24 hrs.)

A

Creatine Kinase

328
Q

Highest elevation of total CK

A

Duchenne’s muscular dystrophy 50-100X than normal value

329
Q

Methods of determination of CK

A

Tanzer-Gilvarg assay (forward direct method)
Oliver-Rosalki Method (Reverse/Indirect method)

330
Q

o pH 9.0 at 340 nm
o Creatine + ATP → CPK → Creatine PO4 + ADP
o ADP + phosphoenolpyruvate → PK → Pyruvate + ATP
o Pyruvate + NADH → LD → Lactate + NAD

A

Tanzer-Gilvarg assay

331
Q

o pH 6.8 at 340 nm;
o most commonly used; faster reaction by 6 times
o Creatine PO4 + ADP → CPK → Creatine + ATP
o ATP + Glucose→ HK → ADP + glucose-6-PO4
o Glucose-6-PO4 + NADP → G-6-PD → 6-phosphogluconate +
NADPH

A

Oliver-rosalki method

332
Q

Anticoagulant that inhibits CK action

A

Oxalates and fluoride

333
Q

CK-BB bounds to

A

IgG

334
Q

CK-MM bounds to

A

IgA

335
Q

An enzyme that catalyzes the interconversion of lactic and pyruvic acid

A

LDH

336
Q

LD1

A

HHHH:H4

337
Q

LD2

A

HHHM:H3M

338
Q

LD3

A

HHMM:H2M2

339
Q

LD4

A

HMMM:HM3

340
Q

LD5 (PINAKA MASARAP)

A

MMMM:M4

341
Q

LD6

A

Alcohol dehydrogenase

342
Q

LD flip pattern

A

LD2 is always higher than LD1 eg. Heart attack, hemolysis in pernicious anemia, and kidney infarction

343
Q

LD flipped pattern in bacterial meningitis and meningococcemia

A

LD4 and LD5 is flipped

344
Q

LD1 and LD2 are seen in?

A

Heart and RBC

345
Q

LD3 is seen in?

A

Lungs, pancreas, spleen, lymphocytes

346
Q

LD4 and LD5

A

Skeletal muscle, liver, intestine

347
Q

Reference Values of LDH

A

o 100-225 U/L (forward reaction)
o 80-280 U/L (reverse reaction)

348
Q

Electrophoresis of LDH from fastest to slowest

A

LD1 > LD2 >LD3 > LD4 > LD5

349
Q

Normal LDH in serum

A

LD 2 > LD 1 >LD 3 > LD4 > LD5

350
Q

LDH if px has heart attack

A

LD1 > LD 2 > LD 3 > LD4 >LD 5

351
Q

LDH if px has bacterial infection

A

LD2> LD1 > LD3 > LD5 > LD4

352
Q

LD6 (alcohol dehydrogenase will only be seen if the patient is

A

Close to death

353
Q

Highest level of LDH is seen in

A

Pernicious anemia and hemolytic disorder

354
Q

10 fold increase especially LD5 which is markedly increased

A

Hepatic carcinoma and toxic hepatitis

355
Q

2-3x increased

A

Viral hepatitis and cirrhosis

356
Q

Methods of determination of LDH

A

Wacker method (forward/direct method)
Wrobleuski-Ladue (reverse reaction)

357
Q

Involved in the transfer of an amino group between aspartate and alpha ketoacids with the formation of oxaloacetate and glutamate

A

AST

358
Q

Highest concentration of AST is found in the

A

liver and cardiac tissue and skeletal muscle

359
Q

Reference value of AST

A

5-37 U/L

360
Q

Method of determination of AST

A

Karmen method - uses malate dehydrogenase and monitors the change in absorbance

361
Q

Catalyzes the transfer of amino group from ALANINE to ALPHA KETOGLUTARATE

A

ALT

362
Q

Reference value of ALT

A

6-37 U/L

363
Q

Method of determination of ALT

A

Reitman-Frankel method

364
Q

Highest concentration of ALT

A

Liver

365
Q

Enzyme involved in the cleavage of phosphate containing compounds in alkaline pH

A

ALP

366
Q

Placental isoenzyme is highest at ___-____the week of gestation

A

16-20th

367
Q

Reference value of ALP

A

30-90

368
Q

Liver ALP is inhibited by

A

Levamisole

369
Q

Most heat labile and inhibited by 5M urea and levamisole

A

Bone ALP

370
Q

Most heat stable (60-65C) and inhibited by phenylalanine reagent

A

Placental ALP

371
Q

Inhibited by phenylalanine reagent

A

Intestinal ALP

372
Q

lung, breast, ovarian and gynecological cancers; bone ALP co-migrator; most heat stable, inhibited by phenylalanine reagent

A

Regan ALP

373
Q

Adenocarcinoma of the pancreas and bile duct, pleural cancer, variant of Regan; inhibited by L-leucine and phenylalanine

A

Nagao ALP

374
Q

Hepatoma/Hepatocellular carcinoma

A

Kasahara ALP

375
Q

ALP is highest in?

A

Paget’s disease (bone disease)

376
Q

Method of determination of ALP

A

Bowers and Mc Comb - ph 10.15 405nm

377
Q

End product and substrate of Klein, Babson, and Reid

A

o Substrate: Buffered phenolphthalein phosphate
o End Product: Free phenolphthalein

378
Q

End product and substrate of Moss

A

o Substrate: Alpha-naphthol phosphate
o End Product: Alpha-naphthol

379
Q

End product and substrate of Huggins and Talalay

A

o Substrate: Phenolphthalein diphosphate
o End Product: Phenolphthalein red

380
Q

End product and substrate of Bessey, Lowry and Brock, Bowers and Mc Comb

A

o Substrate: p-nitrophenyl phosphate
o End Product: p-nitrophenol or yellow nitrophenoxide ion

381
Q

End product and substrate of King and armstrong

A

o Substrate: Phenylphosphate
o End Product: Phenol

382
Q

End product and substrate of Bodansky, Shinowara, Jones, Reinhart

A

Substrate: Beta-glycerophosphate
o End Product: Inorganic phosphate + glycerol

383
Q

Heat stable to heat labile

A

PlaINLiBo (Promise ikaw lang baby)
Placenta, Intestine, Liver, Bone

384
Q

Electrophoresis pattern of ALP

A

LiBoPlaIn

385
Q

Most important activator of ALP

A

Magnesium

386
Q

Reference method for measurement of total ALP

A

Bower’s mccomb PNPP

387
Q

Diagnostic significance of ACP

A

Detection of prostatic carcinoma

388
Q

Used in the investigation of rape

A

ACP

389
Q

Method of determination of ACP

A

Shinowara
Babson, read, and phillips
Roy and HIllman
Gutman and gutman

390
Q

Test for alcoholic abuse

A

GGT

391
Q

Major source of GGT

A

Liver damage (Chronic cholestasis)

392
Q

Obstructive jaundice increases GGT by

A

10 times

393
Q

Hepatobillary damage

A

ALP and GGT

394
Q

Hepatocellular damage

A

ALT and AST

395
Q

Catalyzes the starch into dextrin

A

Amylase/Diastase

396
Q

Smallest enzyme and earliest pancreatic marker

A

Amylase

397
Q

Salivary amylase

A

Ptyalin (s-type)

398
Q

Acinar cells of the pancrease for conversion of dextrine to maltose

A

Amylopsin (P-type)

399
Q

Reference method for amylase determination

A

Saccharogenic method

400
Q

AMYLASE DETERMINATION

A
  • Saccharogenic – measures the amount of reducing sugars produced by
    the hydrolysis of starch
  • Amyloclastic – amylase activity is evaluated by following the decrease
    in substrate concentration
  • Chronometric – measures the time required for amylase to be
    completely hydrolyzed
  • Amylometric – measures the amount of starch hydrolyzed in a fixed
    period of time
401
Q

Activators of amylase

A

Calcium and Chloride

402
Q

Hydrolyzes the ester linkage of fats

A

Lipase

403
Q

Most specific pancreas marker

A

Lipase

404
Q

Lipase determination method

A

Cherry Crandall Method uses olive oil

405
Q

Bilirubin transport deficit

A

Gilbert’s syndrome

defective ligandin = increase B1

406
Q

Conjugation deficit syndrome

A

Crigler-Najjar syndrome

B1 cannot be converted to b2
Increase B1

407
Q

Bilirubin excretion deficit

A

Dubin-Johnson syndrome

B2 cannot be excreted to bile
Elevated b2

408
Q

Familial form of unconjugated hyperbilirubinemia

A

Lucey-Driscoll syndrome

UDPGT inhibitor is circulating
Elevated B1

409
Q

Mixed hyperbilirubinemia

A

Rotor syndrome
Autosomal recessive
Elevated B1 and B2

410
Q

Deficiency of enzyme glucoronyl transferase (low UDGPT)

A

Physiologic jaundice of the newborn
cause kernitcerus
Elevated b1
Nawawala din kasi normal

411
Q
A

MTAP 1 (22 decks)

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