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Michelle: Clinical Chem > Week 1: Amino Acids + Proteins > Flashcards

Week 1: Amino Acids + Proteins Flashcards

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1
Q

How many amino acids (aa) are there in humans?

A

20

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2
Q

What is an essential amino acid?

A

You must eat it

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3
Q

What is the net charge of an aa?

A

Neutral

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4
Q

What is a peptide bond?

A

Amino group of one aa bonds with the carboxyl group of another aa

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5
Q

What is a zwitterion?

A

Have positive and negative charges but net neutral, like aa

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6
Q

What properties does the secondary protein structure add?

A

Strength + flexibility

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7
Q

What properties does the tertiary protein structure add?

A

Shape + function

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8
Q

Describe protein digestion

A
  1. Swallow food, which travels down esophagus to stomach
  2. Stomach pepsin + HCl breaks protein down into peptides
  3. Intestinal enzymes (trypsin, chymotrypsin, elastase, sodium bicarbonate) digest peptides into aa
  4. Amino acids from intestine get reabsorbed into bloodstream to get recycled
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9
Q

What is an aminoacidopathy?

A

Inherited enzyme defect that inhibits the metabolism of certain aa

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10
Q

List aminoacidopathies

A
  • Maple syrup urine disease (MSUD)
  • Phenylketonuria (PKU)
  • Tyrosinemia
  • Alkaptonuria
  • Isovaleric acidemia
  • Homocystinuria
  • Citrullinemia
  • Argininosuccinic aciduria
  • Cystinuria
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11
Q

Blood samples should be drawn after at least what time frame of fasting?

A

6-8 hr fast

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12
Q

How are samples collected for aa analysis?

A

Heparin tube. Plasma removed promptly from cells. Leave buffy coat alone

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13
Q

Deproteination must occur within _____ of sample collection

A

30 min

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14
Q

If analysis cannot be performed immediately, how do you store aa sample?

A

Freeze -20°C to -40°C

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15
Q

Properties of proteins

A
  • 6k to 1 million Da
  • Small is less than 20k Da
  • Variable solubility
  • Electrical charge
  • Adsorption
  • Specific binding to antibodies
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16
Q

What makes proteins more easy to dissolve?

A

More positive charge

17
Q

Carbs and lipids lack which element?

A

Nitrogen

18
Q

Contrast globular and fibrous proteins

A

Globular: symmetric, soluble in saline, (albumin, globulins, histones, protamines)
Fibrous: asymmetric, water insoluble, (collagens, elastins, keratins)

19
Q

List conjugated proteins

A
  • Nucleoproteins (DNA + RNA)
  • Mucoproteins (carbs > 40% wt)
  • Glycoproteins (carbs 10-40% wt)
  • Lipoproteins (cholesterol, triglyc, phospholipids)
  • Metalloproteins (heme)
  • Enzymes (aminotransferase, phosphatase)
  • Hormones
  • Ig
20
Q

What is total protein made of?

A

Total protein = albumin + globulins

  • 54% albumin
  • 46% globulin
21
Q

Total protein reference range

A

6.5-8.3 g/dL

22
Q

Albumin reference range

A

3.5-5.5 g/dL

23
Q

Factors that affect protein concentration

A
  • Nutritional status
  • Physiologic changes
  • Synthesis rate
  • Extracellular distribution
  • Clearance rate
24
Q

Most common cause of hyperproteinemia?

A

Dehydration

Also increased protein production

25
Q

A/G reference range?

A

1.1:1.8

26
Q

List all the globulins

A
  • alpha-1 antitrypsin
  • alpha-2 macroglobulin
  • haptoglobin
  • ceruloplasmin
  • transferrin
  • fibrinogen
  • CRP
  • Myoglobin
27
Q

Categorize each globulin as positive or negative APP

A

Positive APP: alpha-1 antitrypsin, alpha-2 macroglobulin, haptoglobin, ceruloplasmin, CRP

Negative APP: transferrin

28
Q

Cause of hypoproteinemia?

A
  • Negative nitrogen balance
  • Accelerated protein degradation
  • Reduced synthesis/intake
  • Excessive loss
29
Q

List methods of protein analysis

A
  • Total nitrogen
  • Total protein (serum)
  • Salt fractionation
  • Albumin
  • Total globulins
  • Electrophoresis
30
Q

In which conditions is urine protein (microprotein) elevated?

A
  • Kidney failure
  • Nephrotic syndrome
  • Glomerulonephritis
31
Q

CSF protein reference range?

A

15-60 mg/dL

32
Q

CSF produced and reabsorbed by?

A

Produced by choroid plexus cells and reabsorbed through arachnoid

33
Q

CSF protein composition?

A

95% plasma protein, 5% synthesized protein

34
Q

Most common test on CSF?

A

Protein + glucose

35
Q

Describe lab findings in Wilson’s disease pts

A
  • Reduced ceruloplasmin levels
  • Increased serum and urinary copper concentrations
  • Cu deposited in liver, brain, cornea…etc
36
Q

HS-CRP can help evaluate risk of what?

A

Heart disease

37
Q

Function of myoglobin? Toxicity? Where is it found?

A
  • Functions to store oxygen intracellularly
  • Nephrotoxin that can lead to renal failure
  • Mainly striated skeletal and cardiac tissue

Michelle: Clinical Chem (4 decks)

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