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Biochemistry > Unit 3 - Protein > Flashcards

Unit 3 - Protein Flashcards

1
Q

Primary Structure

A

Amino acid sequence determined by DNA

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2
Q

Secondary structure

A

more complex a.a. chain

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3
Q

Tertiary structure

A

Complex folding, 3D structure

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4
Q

Quaternary Structure

A

More than on protein chain

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5
Q

When is biological activity lost in a protein?

A

When secondary/tertiary/quaternary structure denatured

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6
Q

Simple protein

A

No other major chemical class associated with them

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7
Q

Conjugated proteins

A

Nonamino acid chemical associated with protein
(prosthetic group)

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8
Q

Lipoprotein

A

proteins with fat
(cholesterol, triglyceride, phospholipids)

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9
Q

Metalloproteins

A

Contain a metal
(hemoglobin)

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10
Q

Glycosylated proteins

A

Contain carbohydrate
(HgbA1c)

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11
Q

Types of measurement methods

A

Light absorption
Light refraction
Dye bonding/Colorimetric
Electrophoresis

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12
Q

215nm

A

Peptide bond

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13
Q

280 nm

A

Aromatic rings present in a.a.

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14
Q

What proteins are detected at 280 nm?

A

Tyrosine
Tryptophan
Phenylalanine

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15
Q

What measurement method is best for a known or pure protein?

A

Light absorption

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16
Q

What measurement method is nondestructive for proteins?

A

Light absoprotion

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17
Q

What is a total protein measurement that is rapid?

A

Light refraction

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18
Q

What specimen is worst for light refraction?

A

CSF
Low protein specimen

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19
Q

What are the physical properties used to detect and measure proteins

A

Molecular size
Electrical charge
Solubility

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20
Q

What affects electrical charge?

A

pH

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21
Q

How does solubility measure proteins

A

A protein is dissolved or precipitated out of a mixture

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22
Q

What is used to manipulate solubility

A

SUlfosalicylic acid

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23
Q

What does increased turbidity mean for a solubility sample?

A

More protein was precipitated out

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24
Q

What are the major components of biuret?

A

Sodium Hydroxide + Copper sulfate

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25
Q

What dye bonding test is used to measure total protein

A

Biuret

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26
Q

What dye bonding test is used to measure albumin?

A

BCG
BCP

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27
Q

How does biuret work to bond to the protein?

A

Copper ions react with carbonyl oxygen and amide nitrogen in peptide bond

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28
Q

How many peptide bonds are required for biuret analysis?

A

At least two

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29
Q

Are dipeptides measured by biuret ?

A

No, two amino acids with one peptide bond

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30
Q

What is a positive color change for biuret?

A

Blue biuret makes a violet color with protein

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31
Q

Color intensity increases as ___ increases

A

Peptide bonds amount

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32
Q

Total protein reference range in serum

A

6-8 g/dL

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33
Q

What’s the difference in tp concentration from serum and other fludis

A

Serum has highest concentration, others are measured in mg or ng quantities

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34
Q

When would a pink color be produced in biuret method

A

In presence of small peptides

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35
Q

How is biuret calibrated?

A

With albumin alone because other protein concentrations are too diverse and unpredictable

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36
Q

What samples are not appropriate for biuret

A

CSF
Urine

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37
Q

What dye is used to measure lower protein levels like in CSF or Urine

A

Coomasie Blue
Ponceau S
Amido black
Pyrogallol red

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38
Q

When is insensitivity in dye bonding for globulins NOT a problem?

A

A leaky glomerulus in the kidney because albumin spills into urine

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39
Q

When is insensitivity in dye ending for globulins a problem?

A

Multiple myeloma because free light chains spill into urine

40
Q

Which test would you choose for clinical decisions based on serum albumin? BCG or SPE?

A

BCG/BCP

41
Q

Total Protein formula

A

Alb + Glob

42
Q

Globulin formula

A

TP - Albumin

43
Q

A/G ratio

A

Albumin divided by globulin

44
Q

Albumin reference range in serum

A

3.5-5 g/dL

45
Q

Globulins reference range in serum

A

2.5-3 g/dL

46
Q

Protein reference range in urine

A

1-14 mg/dL
<100 mg/24 hours

47
Q

Protein reference range in CSF

A

15-45 mg/dL
Note small window

48
Q

Calculation of protein in urine using 24 hours specimen

A

(given total protein mg/dL divided by 100mL) = (xmg/given total mL)

49
Q

What urine specimen eliminated biological variation and dilution effects?

A

24 hour urine

50
Q

Why would 24 hour urine be required?

A

Evaluate urine and eliminate biological variation and dilution effects

51
Q

What is the point where the number of positive charges equal the number of negative charges?

A

Isoelectric point

52
Q

If the isometric point of albumin is 4.6, what is its charge at 4.6?

A

No net charge
Neutral

53
Q

Albumin Iso point is 4.6, what is its charge at 5.1

A

Positive charge

54
Q

What is the isoelectric point of globulins

A

5.1-6.2

55
Q

Which protein has the highest net negative charge at a buffer pH of 8.6

A

Albumin

56
Q

What is the usual pH of the buffer for SPE

A

8.6

57
Q

Anode

A

Positive pole

58
Q

Cathode

A

Negative pole

59
Q

Where do anions move?

A

To the anode

60
Q

Where do cations move?

A

To the cathode

61
Q

The more the negative charge, the __ the movement?

A

faster

62
Q

What causes the visible application point on SPE?

A

Precipitated protein from a thawed specimen or debris

63
Q

A molecule has no charge, where will it move in an electrical field?

A

Nowhere

64
Q

What does the buffer make the molecules do?

A

Take on a negative charge to move towards the anode

65
Q

Where is the origin of the application point?

A

Cathode, negative pole

66
Q

Fast equivalent to

A

Positive end

67
Q

Slow equivalent to

A

Negative end

68
Q

Frictional coefficient

A

Medium resists particle movement

69
Q

how do larger, more complex molecules move if the pores in the medium are small?

A

Slowly

70
Q

If the support medium has small pores, what is separation based on?

A

Size and charge

71
Q

If the support medium has large pores, what Is separation based on?

A

Charge only

72
Q

High voltage can cause

A

High temps that denature proteins

73
Q

Usually, the slab or room should be…

A

Cold

74
Q

What is the standard buffer for SPE?

A

Sodium barbital required for electrons to flow

75
Q

What kind of ionic strength do you want your buffer to have?

A

Low, the extra ions will impede migration by adding charge

76
Q

What is wick flow caused by

A

Evaporation of the buffer

77
Q

What does wick flow look like

A

Proteins make a trail

78
Q

How do you fix wick flow

A

Cool the system or buffer
Keep lid on electrophoresis chamber
Change buffer/use new buffer every time

79
Q

What is electroendosmosis

A

Weak anions bump into strong cations and move behind the application point

80
Q

Tracer dyes

A

Stick to albumin and make the band look fat

81
Q

Two albumin bands can be caused by

A

Genetic bisalbuminemia
or
Drugs

82
Q

Why would drugs cause two albumin bands

A

They can bind to the albumin

83
Q

Split beta bands have

A

Transferrin and C3

84
Q

If a split beta gel wasn’t being used, what would the C3 band make you think?

A

If the peak is a monoclonal spike
or
If specimen is fresh

85
Q

What does fresh specimen look like eon SPE?

A

Monoclonal spike in beta band, split beta band

86
Q

What does fibrinogen do to SPE

A

Looks like a spike if plasma used

87
Q

Where does fibrinogen migrate to on SPE

A

Between beta and gamma

88
Q

How to solve the spike caused by fibrinogen?

A

Allow serum to fully clot
Add thrombin so blood will clot (if can’t be recollected)

89
Q

Where does hemolysis appear on SPE?

A

Between a2 and B

90
Q

What Ig are most commonly seen on SPE?

A

G, A, M

91
Q

Why aren’t IgD or IgE seen on SPE?

A

Too low concentration, unless monoclonal

92
Q

Where does CRP appear on SPE

A

Gamma region toward beta side

93
Q

When would CRP be elevated on SPE?

A

Acute phase reactant
May mimic monoclonal spike

94
Q

Isoelectric focusing

A

Electrophoresis done in pH gradient

95
Q

How does isoelectric focusing work

A

Proteins stop moving when they reach the pH of their isoelectric point

Biochemistry (26 decks)

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