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Test 2 Flashcards

1
Q

How are proteins formed?

A

Amino acids link head-to-toe (amino group to carboxyl group)

This bond releases water

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2
Q

What are the 4 levels of structure in a protein?

A

Primary- type of amino acids

Secondary- winding pattern of chain

Tertiary- the way the chain folds and bends 3 dimensionally. Most properties come from this level

Quaternary- uncommon, two or more chains joining together like snakes

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3
Q

What is denaturation?

A

Loss of secondary, tertiary, or quaternary structure

Caused by heat, acids & bases, enzymes, UV light

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4
Q

What are some key characteristics of proteins?

A

Large
Can be conjugated with other organic molecules (lipoproteins, glycoproteins, etc)

High specificity- making them immunogenicity and easy to detect

Maintains pH (buffer)

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5
Q

Do proteins dissolve well?

A

No, they are colloidal because they have a charge as well as a water pocket surrounding them

Solubility can be altered by ph, ionic strength, temperature, and dielectric constant

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6
Q

What are ampholytes?

A

Compounds with both acid and base (dipolar)

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7
Q

What is an amphoteric compound?

A

Compounds which behave as an acid and a base concurrently

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8
Q

What is a zwitterion?

A

Characteristic pH for each AA where positive charge and negative charge are equal

(Occurs at isoelectric point)

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9
Q

What are the implications of zwitterions?

A

When put in basic solution, charge will be negative

When put in low ph, charge will be positive

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10
Q

What are the main functions of proteins?

A

Structure, enzymes, hormones,electrolyte/water balance, transport, defence, energy, coagulation. Buffer

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11
Q

What is salts effect on proteins?

A

High salt concentration- less water avian able for protein, stronger protein-protein bond, weaker protein-water bond (salting out)

Salting in is opposite

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12
Q

How do organic solvents (alcohols etc) affect solubility of proteins?

A

Alcohols and other organic compounds bind to water, so protein can’t

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13
Q

What is important about protein metabolism?

A

They are too big for us to use upon eating them , must be broken down

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14
Q

What happens with excess proteins?

A

Stored in nitrogen pool after being converted into biologically useful molecules

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15
Q

What is the process of protein digestion?

A

In stomach, pepsinogen (excreted by chief cells) meets HCl and becomes pepsin

Pepsin begins protein breakdown and converting even more pensinogen (autocatalysis)

In small intestine, proteolytic enzymes break down proteins into amino acid

Amino acids absorbed in small bowel to portal vein

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16
Q

What is protein synthesis

A

Formation of tissue proteins, enzymes, hormones, antibodies, and plasma proteins from amino acid pool

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17
Q

What is decarboxylation

A

Loss of CO2 from an amino acid

Generates an amine which can be used to form non-protein nitrogen compounds (like nucleic acids)

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18
Q

What is deamination?

A

Oxidative- splitting off of amino group from amino acid- forming ketone acid and ammonia

Transamination- reversible transfer of amino acid group from amino acid to keto acid

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19
Q

Ammonia from deamination

A

Product of oxidative

Toxic in high concentrations- CNS disruption

Removed by the ORNITHINE cycle- ammonia to urea (in liver)

Liver damage- difficulty converting ammonia to urea

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20
Q

Normal serum protein level

A

60-80g/L

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21
Q

Five major serum proteins

A

Alpha 1 globulins- 1-4 g/L (LIVER)

Alpha 2 globulins-4-8 g/L (LIVER)

Beta globulins- 5-10 g/L (LIVER)

Gamma globulins- 6-13g/L (bone marrow)

Albumin- 35-47g (tiny) (LIVER)

Fibrinogen- only in plasma 2-4.5 g/L (LIVER)

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22
Q

AG ratio

A

Number obtained when total albumins divided by total globulin

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23
Q

Hypoproteinemia and hyperproteinemia

A

Hypo- under 60

Hyper- over 80

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24
Q

Are serum proteins positive or negative?

A

Negative in blood

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25
What are the two types of AA abnormalities?
Overflow(primary)- renal threshold exceeded Renal type- defects in kidney cause release of AA
26
Methods of protein measurement
Immunochemical- antibodies Elecrophoresis- proteins carry charge Quantitative Mass Spectrophotometry and ultraviolet absorption
27
Specimen requirements protein
Non hemolyzed, cell free serum, urine OR CSF Stored 2-8 for up to 3 days
28
Biuret method
Under high pH copper binds with nitrogen in proteins, making red colour 550 nm Needs di peptide structure and three amino acids (no albumin) Not sensitive enough for CSF or URINE Lipemia, hemolysis, bilirubin interfere More peptide bonds= darker colour
29
Do biuret methods require fasting?
No, but lipemia may occur
30
Normal urine protein values
Per day- 50-80mg 24hr- 10-140 mg/l CSF value is 15-45mg/dL
31
Scattered light methods
Used for small concentrations Uses turbidity (based on light scattered by beam) Must be precipitated before measurement Not usually done on urine
32
Advantages and disadvantages of turbidimetric methods
Can detect low levels (250-900mg/L) Measures turbidity from every source
33
Refractometry
Protein changes direction of light Measuring total solids, not just proteins Not sensitive (only over 35g/l) Not specific Used solely for serum
34
Dye binding
May be sued for serum, urine, and CSF PH of solution used for albumin makes it positively charged, dye is negatively charged to attach
35
Urine dipsticks
Most tests adhere to albumin because it's positive Can get false positive from other proteins, or chemical interference affecting pH of urime False negatives if acid has been added to preserve
36
Identification of specific proteins
Ultracentrifuge- arranges them by size Immunochemical- specific antibodies Chromatography- Salting out- can separate albumin from globulins Dyes Electrophoresis- most common
37
What are proteins
Organic substances only soluble in non-polar substances
38
Main functions of fat
Energy (9.3 calories/g) Insulation Neurological conductor Steroids Membrane formation Can be adipose or working lipids(tissue)
39
Major lipids of body
Triglycerides, cholesterol, phospholipids, glycolipids
40
What are the two classifications of lipids?
SIMPLE CHO Neutral fats and triglyceride Triglyceride- glycerol and 3 fatty acids If 3 same- simple trig, if 3 different, mixed trig COMPOUND CHO and others phospholipids, glycolipids, etc
41
Lipoprotein
Hydrophobic core of trig or chol surrounded by phospholipids, chol B/c can't be freely in plasma
42
Chylomicron
Specific lipoprotein that transports from small intestine to tissues (very small)
43
Atherosclerosis
Yellow plaque buildup of lipids in medium and large arteries
44
Cholesterol
Essential component in lipid metabolism We consume this
45
Triglyceride
Simple lipid made of three fatty acids estrogen into glycerol
46
Why are lipids important
Necessary for transporting energy around the body
47
Lipid metabolism
Mostly digested in small intestine Emulsified in stomach Mixed in small intestine with bike from liver which emulsifies and activated lipase Lipase secreted by pancreas Fats transported as small water soluble fragments liver and tissues via lymph and blood Lipids can also be formed by carbs and proteins
48
Livers role in fat digestion
Releases bile for fat emulsification
49
What are chylomicroms
Responsible for lipemia Transport fat from gut to adipose, liver, and muscle
50
Lipid metabolism for energy
Fatty acid spiral- beta oxidation to remove two carbons and produce ATP
51
Excess ketones
Acidosis can occur if happening too fast Occurs b/c low carbs
52
What is cholesterol
Steroid alcohol 70-80% esterified (one fatty acid molecule) 20-30% free Used to manufacture and rapid membranes, produces bile acids Transports fats as wax, helps with muscle contraction
53
How does cholesterol enter body
In animal products Some absorbed by intestine Liver synthesizes, estrified, and converts cholesterol into bile acids Liver damage decreases chol level Transported around body as lipoprotein
54
What are the 4 types of lipoproteins
HDL- high dENSITY LDL- low density IDL- intermediate density VLDL- very low density
55
Cholesterol levels
1-30 years 2.6a5.2 mmol/l Over 60. Less than 6.2 Newborns- 1/3
56
What are causes of abnormal serum cholesterol
Familial hyperlipoproteinemia- hereditary Postmenopausal- low estrogen Jaundice Hypothyroidism Low cholesterol may be due to liver disease, hyperthyroidism
57
VLDL
Very bad Right in trig More fat than protein
58
LDL
Bad Contains most cholesterol (50%) Transports cholesterol from liver to tissues High association with CHD
59
HDL
Smallest of lipoproteins Made by liver and intestine Takes away excess chol and returns to liver
60
Types of atherosclerosis
Peripheral vascular disease- arms or legs Coronary artery disease- heart Cerebrovascular disease- brain, stroke
61
How does plaque buildup happen?
Small vessel injuries occur normally, Lola brings cholesterol For repair, cells accumulate below endothelial layers
62
Primary atherosclerosis causes
Genetics Hypertension- extra pressure on arteries Smoking- increases LDL Elevated total cholesterol Decreased HDL
63
Secondary atherosclerosis causes
Lack of exercise Obesity Male Age Stress Diabetes mellitus Gout Renal failure
64
Lipid testing method
Measures triglycerides Cholesterol Lipoproteins SHOULD BE FASTING for trig and chol CALLED LIPID PROFILE (serum)
65
Can all cholesterol be measured?
No, esterified chol (70%) must be converted to free in order to be measured Thus, takes 3 enzyme steps Cholesterol esterase- converts to esters cholesterol oxidase Peroxidase- colour
66
What are fecal samples used for?
Detection of decreased pancreatic function Steatorrhea- increased fat in feces 2-6g
67
What is uric acid
Product of breakdown of adenine and guanine
68
What are two forms of uric acid
Blood- URATE Below 6.0- URIC ACID Uric acid can form crystals- kidney stones
69
What is reabsortbtion of URATE back into blood l
98- 100%
70
Issue with uric acid
Overproduction- increased cell breakdown Decreased renal excretions- kidney disease Congenital enzyme deficiencies Gout- buildup of crystals in joints

Clinical chem (3 decks)

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