CC (midterms) Flashcards
(185 cards)
1
Q
Enzymes
A
Biologic proteins that catalyze the biochemical reactions
Intracellular proteins to hasten the chemical reaction
Affects the reaction of organic matter
Enzymes are not consumed nor altered
Only the substrates changes the form (substrate to product)
2
Q
Increased enzymes in the serum may be because:
A
Cell injury or cell degradation
Increased membrane permeability allowing for proteins to move out of the cell
3
Q
Function of enzymes:
A
Hydration of carbon dioxide during respiration
Nerve induction
Muscle contraction
Nutrient degradation
Growth and reproduction
Energy storage and use
4
Q
LIVER ENZYMES
A
Aspartate aminotransferase (AST)
Alanine aminotransferase (ALT)
Gamma-Glutamyl transferase (GGT)
Alkaline phosphatase (ALP)
Acid phosphatase (ACP)
5
Q
MI Profile
A
Creatine Kinase (CK)
Aspartate Aminotransferase (AST)
Lactate Dehydrogenase (LDH)
6
Q
Pancreatic Enzymes
A
Amylase (AMS)
Lipase (LPS)
7
Q
Prostate enzymes
A
Acid phosphatase (ACP)
Glucose-6-phosphate dehydrogenase (G6PDH)
8
Q
Miscellaneous enzymes
A
- 5’ Nucleotidase (5’N)
- Cholinesterase / Pseudocholinesterase
- Angiotensin-Converting enzyme (ACE)
- Ceruloplasmin
- Ornithine carbamoyl Transferase (OCT)
- Glucose-6-phosphate dehydrogenase (G-6PD)
9
Q
other name for AST
A
Serum glutamic-oxaloacetic transaminase or Serum glutamate-oxaloacetate transaminase (SGOT)
10
Q
Transfer of an amino group between aspartate and a-keto acids
A
AST
11
Q
Involved in the synthesis and degradation of AA (amino acids)
A
AST
12
Q
Widely distributed, highest activities in cardiac, liver and skeletal muscle
A
AST
13
Q
2 isoenzymes of AST
A
Cytoplasmic
Mitochondrial
14
Q
most abundant, the most predominant AST in healthy human serum
A
Cytoplasmic AST
15
Q
present in the mitochondrial membrane. An increase in this isoenzyme indicates possible necrosis or severe damage of the cell.
A
Mitochondrial AST
16
Q
After MI, AST levels begin to rise in ___, peak at ___, and return to normal in ____.
A
6–8 hours; 24 hours; 5 days
17
Q
AST increased in
A
in hepatocellular and skeletal muscle disease
18
Q
Uses malate dehydrogenase and monitors decrease in absorbance at 340 nm
A
Karmen Method
19
Q
method that is falsely ↑ in hemolyzed sample
A
Karmen Method
20
Q
Karmen Method reference range:
A
5-30 U/L
21
Q
Aspartic acid + a-ketoglutaric acid ⇆ ____________
A
glutamic acid + oxaloacetic acid
22
Q
oxaloacetate + NADH + H ⇆ _____
A
malate + NAD
23
Q
are enzymes with similar catalytic activity but differ in the physical, biochemical and immunologic properties.
A
Isoenzymes
24
Q
a type of cofactor that serves as the second substrate for enzymes.
A
Coenzymes
25
When a coenzyme is tightly bound to an enzyme, it is called a ____
prosthetic group
26
Oxidized form: NAD measures for
Decreased absorbance
27
Reduced form: NADH
high/increased absorbance
28
other name for Alanine aminotransferase (ALT)
serum glutamic-pyruvic transaminase (SGPT)
29
Transfer of an amino group between alanine and a-ketoglutarate
ALT
30
more liver specific compared to AST
ALT
31
Increased in hepatocellular disorders
ALT
32
Significant in the evaluation of hepatic disorders
Markedly increased in acute inflammatory conditions of the liver
Used to monitor the course of hepatitis treatment and the effects drug therapy
Used for screening for post transfusion hepatitis
Used to screen blood donors, (ALT increased with people with jaundice)
Used as sensitive test for occupational toxic exposure
Monitors course of hepa treatment and possible effects of drug therapy
uses of ALT
33
The AST/ALT Ratio
Differentiates the cause of hepatic disorder
De Ritis Ratio
34
Ratio > 1
non viral origin
35
Ratio < 1
viral in origin
36
pyruvate + NADH + H ⇆ _____
Lactate + NAD
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pyruvate +glutamate ⇆ _____
alanine + a-ketoglutarate
38
Assay for enzyme activity ALT
Uses Lactate Dehydrogenase and monitors decrease in absorbance at ___
340 nm
39
COLOR DEVELOPER ALT and AST
2,4 DNPH
40
COLOR INTENSIFIER ALT & AST
0.4 N NaOH
41
METHODS for ALT and AST
Reitman and Frankel
42
Catalyze the transfer of the y-glutamyl residue from y-glutamyl peptides to amino acids H2O, etc
Gamma-Glutamyl transferase (GGT)
43
In the biologic system, the common donor for y-glutamyl is _____
glutathione
44
glutathione + amino acid → ___
glutamyl-peptide + L-cysteinyglycine
45
Used for diagnosis hepatobiliary disorders and chronic alcoholism
GGT
46
GGT is located in the ____ of the hepatic cells. Specifically in the epithelial cell linings of _____
canaliculi; biliary ductules
47
Sensitive marker for ethanol intoxication.
Marker for occult alcoholism
GGT
48
Most sensitive marker for acute alcoholic hepatitis
GGT
49
Assay for Enzyme Activity in GGT
Szaz Assay
50
The absorbance of p-Nitroaniline is measured at
405-420 nm
51
y-glutamyl-p-nitroanilide + glycylglycine → ____
y-glutamyl-glycylglycine + p-nitroaniline
52
Involved in the storage of high-energy creatine phosphate in muscle cells
Creatine Kinase (CK) or Creatine Phosphokinase (CPK)
53
CK is widely distributed, highest activities in _____.
skeletal muscle, heart and brain.
54
creatine phosphate + ADP → ___
creatine + ATP
55
Methods of determination for CK
Forward Reaction (Tanzer-Gilvarg)
Reverse Reaction (Oliver-Rosalki)
56
Optimum pH for Tanzer Gilvarg
9.0
57
Optimum pH for Oliver-Rosalki
6.8
58
↓ in absorbance at 340 nm is determined
Forward Reaction (Tanzer-Gilvarg)
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↑ in absorbance at 340 nm is determined
Reverse Reaction (Oliver-Rosalki)
60
Source of Error for CK
Hemolysis
inactivation by light
Physical activity and IM injections
61
Reference Range of CK (male & female; % of CK-MB)
Male: 15-160 U/L; Female: 15-130 U/L
CK-MB: <6% of total CK
62
Slowest mobility toward the anode
Major isoenzyme in striated muscle and normal serum
Ck-3/CK-MM/
Muscle type
63
2nd fastest to migrate toward the anode
Significant quantities are found in heart tissues
CK-2/CK-MB/
Hybrid type
64
Migrate the fastest toward the anode
Highest concentration in CNS, GI tract and uterus (pregnancy)
CK-1/CK-BB/
Brain type
65
After MI, CK-MB (>6%) levels begin to rise within ___, peak at ____ and return to normal levels within ___
4-8 hours; 12-24 hrs; 48-72 hrs
66
It is the first enzyme to elevate after a myocardial infarction
CK
67
CK is considered a ____ . It is composed of two different monomers. Composed of M and B type
dimeric molecule
68
Reference Values of CKs
CK-MM: 94-98%
CK-MB: 2-6%
CK-BB: <1%
69
Other CK Isoenzymes
Macro-CK
70
CK-BB is complexed with antibodies __
IgG or IgA
71
CK-MM is complexed with ___
lipoproteins
72
macro-CK migrate midway between ___
CK-MM and CK-MB
73
Located in mitochondrial membrane, increase in this indicates cell necrosis or severe damage
Migrates cathodal to CK-MM
Mitochondrial CK (CK-Mi)
74
Where the activity of CK1, CK2 and CK3 are all measured
It is less diagnostic bc it is not tissue specific
Total CK
75
This targets a particular tissue
Improves the test specificity thus improving diagnosis
CK isoenzyme
76
Catalyzed the interconversion of lactic and pyruvic acids
Widely distributed, highest activities in heart, hepatic, skeletal muscle and RBC
Lactate Dehydrogenase (LDH)
77
Is a tetrameric molecule composed of 4 subunits/monomers of 2 possible forms
LDH
78
lactate + NAD → ___
pyruvate + NADH + H
79
Composed of 5 isoenzymes
LDH
80
temp that decreases the activity of LD
low temp/freezer temp
81
temp (+storage) that can maintain the activity of LD
If room temp for 2 days
82
Assay of Enzyme Activity for LDH
Wacker method
Wroblewski La Due
a-hydroxybutyrate dehydrogenase (a-HBD)
83
Reverse Reaction (Pyruvate → Lactate)
Decrease in absorbance is monitored at 340 nm
Three times faster but more susceptible to substrate exhaustion
Wroblewski La Due
84
Optimal pH of Wroblewski La Due
7.1 to 7.4
85
Forward reaction (Lactate → pyruvate)
Increase in absorbance is monitored at 340 nm
Commonly used method in LD
Wacker method
86
Optimal pH of Wacker method
8.3 - 8.9
87
Has greater affinity of H subunits
a-hydroxybutyrate dehydrogenase (a-HBD)
88
Represent LDH-1
a-hydroxybutyrate dehydrogenase (a-HBD)
89
a-ketobutyrate + NADH + H →
a-hydroxybutyrate
90
After MI, LD begin to rise within ____, peak at ____ and remains elevated for ___
10-24 hrs; 48-72 hrs; 10 days
91
Reference range of LD
100-225 U/L
92
LDH is a __ containing two active sub-units
tetramer
93
Order ng pinakamataas sa healthy serum
LD 2 > 1 > 3 > 4 > 5
94
order of LD from most anodic (fastest) to least anodic (slowest)
LD 1 > LD 2 > LD 3 > LD 4 > LD 5
95
🡹LDH 1 & 🡹CK-MB
AMI
96
🡹LDH 1 and normal CK-MB
hemolytic anemia
97
LDH 6 (Alcohol Dehydrogenase) present in px with:
Drug hepatotoxicity
Obstructive Jaundice
Artherosclerotic failure
98
LDH-1 and LDH-2 tissue involved
Heart, RBC
1 - (MI, hemolytic anemia)
2 - (RI, megaloblastic anemia)
99
LDH-3
Lung, Spleen, Pancreas (Pulmonary embolism)
100
LDH-4
Liver (Hepatic injury)
101
LDH-5
Skeletal Muscle (Skeletal muscle injury)
102
Catalyze the hydrolysis of various phosphomonoesters at an alkaline pH
Liberate inorganic phosphate from an organic phosphate ester with production of alcohol
Alkaline phosphatase (ALP)
103
Sources of ALP
Sources: Liver, Bone (Osteoblast), Placenta, Intestine, Renal tissues
104
Requires Mg2+ activator
For evaluation of hepatobiliary and bone disorders
ALP
105
Reference Range of ALP
30-90 U/L (adult)
70-220 u/L (0-3 months)
50-260 U/L (3-10 years)
60-295 U/L (10-puberty)
106
Assay for enzyme activity
in ALP
Bowers and McComb
107
Based on molar absorptivity of P-Nitrophenol at a pH of 10.2
Absorbance is measured at 405 nm (visible light region)
Bowers and McComb
108
p-nitrophenyl-phosphate (colorless) → ___
p-nitrophenol + phosphate ion (yellow)
109
methods with β-glycero-phosphate as substrate
Bodansky
Shinowara
Jones
Reinhart
110
methods with P-nitrophenyl phosphate as substrate
Bessy, Lowry & Brock
Bowers & McComb
111
method in which phenyl phosphate as substrate
King and Armstrong
112
methods where
Inorganic PO4 + Glycerol as end product
Bodansky
Shinowara
Jones
Reinhart
113
P-nitrophenol (yellow)
as end product
Bessy, Lowry & Brock
Bowers & McComb
114
end product of King and Armstrong
Phenol
115
ALP Isoenzymes:
Electrophoresis
116
Electrophoresis - Arranged by most anodal (fastest)
1. Liver ALP - fastest
2. Bone ALP
3. Placental ALP
4. Intestinal ALP
117
Heat labile fraction
🡹 in bone disease, healing of bone fractures, and physiologic bone growth
Bone ALP
118
Fastest Isoenzyme and 🡹 in liver disease
Two fractions: Major liver & fast liver (a1) band
Liver ALP
119
Most heat stable fraction and 🡹 in pregnancy
Can withstand heating at 65degC for 30 mins
Placental ALP
120
Slowest moving fraction, in blood groups B or O
🡹 in fatty meal consumption and GIT disorders
Intestinal ALP
121
Chemical inhibition in ALP:
Phenylalanine
Placental, Intestinal (Putang Ina)
122
Chemical inhibition in ALP:
Levamisole
Bone, Liver (Blood Lust ♥)
123
Chemical inhibition in ALP:
.03 moral urea
Bone (only one to be inhibited)
124
ALP isoenzyme differentiation by Heat stability
Placental ALP (most stable)
Intestinal ALP
Liver ALP
Bone ALP (least stable)
125
Total ALP elevations by liver or bone ALP is differentiated by heating of serum at ___
56degC for 10 mins
126
ALP residual activity is ⬇ decrease to >20%
Liver ALP
127
ALP residual activity is ⬇ decrease to <20%
Bone ALP
128
Carcino Placental ALP
Regan ALP:
Nagao ALP
129
Carcino Placental ALP Inhibitors:
phenylalanine, L-leucine
130
Most heat stable ALP
Lung, Breast, and Gynecological cancers, bone ALP co-migrator,
Regan ALP
131
Adenocarcinoma of the pancreas and bile duct, pleural cancer
Nagao ALP
132
INHIBITED BY:
Phenylalanine
L-leucine
Nagao
133
INHIBITED BY:
Phenylalanine
Regan
134
Catalyze the hydrolysis of various phosphomonoesters at an acid pH
Liberate inorganic phosphate from an organic phosphate ester with production of alcohol
Acid phosphatase (ACP)
135
Acid phosphatase is present in the ff tissue source:
Prostate
Red blood cells
Platelets
Bone
136
For evaluation of metastatic carcinoma of prostate
Forensic investigation of rape
ACP
137
inhibits specific prostatic ACP
L-tartrate ions
138
Reference Range: Prostatic ACP:
0-3.5 ng/ml
139
Quantitative end point substrate
Thymolphthalein monophosphate
140
Continuous monitoring substrate
α-napthyl phosphate
141
Gutman and Gutman substrate and end product
Phenyl PO4;
Inorganic phosphate
142
Shinowara substrate and end product
PNPP;
P-Nitrophenol
143
Babson, Read, and Phillips substrate and end product
Alpha naphtyl PO4;
Alpha naphthol
144
Roy and Hillman substrate and end product
Thymolphthalein MonoPO4
Free thymolphthalein
145
where pancreatic enzymes r produced
acinar cells of the pancreas
146
An example of HYDROLASE
Promotes breakdown of starch and glycogen via alpha, 1-6 branching linkages
Amylase (AMS)
147
Major tissue source of AMS
Pancreas
Salivary gland
148
Minor tissue source of AMS
Adipose tissues
Fallopian tube
Small intestine
Skeletal muscle
149
Increased in acute pancreatitis, renal failure, and parotitis
Is the smallest enzyme
The first enzyme to increase in acute pancreatitis
AMS
150
Amylase increases after ____, the peak is after ___. The level persists for .
2-12 hours; 24 hours; 3-5 days
151
Salivary amylase - __
ptyalin (fast moving)
152
Pancreatic amylase -__
amylopsin (slow moving)
153
The activity of amylase is inversely proportional with the absorbance
Measures the disappearance of starch substrate
Starch-Iodine complex (dark-blue) 🡺 Decrease in color intensity (decreased absorbance)
Amyloclastic
154
Measures the appearance of the product
Starch 🡺 reducing sugars
Directly proportional of amylase activity with the absorbance
Saccharogenic
155
Measures the increasing color from production of product-chromogenic dye fragment
Insoluble starch-dye 🡺 double starch-dye fragments
Amylase activity is directly proportional to the starch-dye fragment formation
Chromogenic
156
Coupling of several enzyme systems to monitor amylase activity
The end product is the 5,6-phosphogluconolactone + 5 NADH (🡹 absorbance)
Continuous monitoring
157
maltopentose → ___
maltrotriose + maltose
158
Not excreted and is reabsorb in the plasma
Presence of macroamylase in the plasma
Amylase with antibodies
Macroamylasemia
159
Hydrolyzes the ester linkages of fats to produce alcohols and fatty acids
Hydrolysis of dietary triglycerides in the intestine to 2-monoglyceride and fatty acids
Lipase (LPS)
160
Specific for pancreatitis
But in time of elevation, amylase is faster than ___
LPS
161
2-monoglyceride + 2 fatty acids → ___
triacylglycerol + 2H2O
162
Larger molecule and remains longer in circulation (7 days)
LPS
163
Assay for enzyme activity LPS
Estimation of liberated fatty acids
Measurement of the amount of light blocked by the suspension or particles in soluble agents in the sample.
Turbidimetric methods
164
method where phenolphthalein as indicator for LPS
Cherry Crandall
165
Tietz indicator
Thymolphthalein + Veronal
166
end color of Cherry Crandall
Pink
167
end color of Tietz
Blue
168
Cherry Crandall & Tietz's substrate
50% olive oil (triolein)
169
titrating agent for Cherry and Tietz
0.4N NaOH
170
end point of Cherry and Tietz
Fatty acid (Oleic acid)
171
A phosphoric monoester hydrolase
Marker for hepatobiliary disease and lesions of liver
Reference value: 0-1.6 units
5’ Nucleotidase (5’N)
172
Used as a marker for insecticides/pesticides poisoning
Index of parenchymal function
Cholinesterase / Pseudocholinesterase
173
Used to monitor the effect of muscle relaxants (succinylcholine) after surgery
Reference value: 0.5 - 1.3 Units (plasma)
Cholinesterase / Pseudocholinesterase
174
Used as a possible indicator of neuronal dysfunction (ptx w/ alzheimer’s disease)
Conversion of Angiotensin 1 to 2 happens in the lungs
Angiotensin-Converting enzyme (ACE)
175
A.K.A. Peptidyl Dipeptidase A or Kininase II
Increased in: Sarcoidosis, Acute and Chronic Bronchitis, and Leprosy
Angiotensin-Converting enzyme (ACE)
176
main source of ACE
Main source: Macrophage and Epithelioid cells
177
Promotes the vasoconstriction of the renal arterioles to promote increase BP
Stimulates the release of aldosterone
Angiotensin II
178
Copper-carrying protein which acts as a na enzyme
A marker for wilson’s disease (hepatolenticular disease)
Ceruloplasmin
179
For hepatobiliary diseases
Reference values: 8-20 mU/ml
Ornithine carbamoylTransferase (OCT)
180
maintains the NADPH in the reduced form in erythrocytes
a newborn screening marker
Glucose-6-phosphate dehydrogenase (G-6PD)
181
Maintains the NADPH in the reduced form in the erythrocytes
A newborn screening marker
Glucose-6-phosphate dehydrogenase (G-6PD)
182
Deficiency can lead to drug-induced
Specimen: red cell hemolysate, serum
Reference value : 10-15 U/g Hgb or 1200-2000 mU/mL packed RBC
Glucose-6-phosphate dehydrogenase (G-6PD)
183
Glucose-6-phosphate dehydrogenase (G-6PD) is found in the
adrenal cortex, spleen, rbc, and lymph nodes
184
Increased levels of G6PD can be seen in conditions like:
AMI, megaloblastic anemia
185
inhibits red cell ACP
Formaldehyde & Cupric ions
