Unit 3 - Redone Flashcards

1
Q

Primary Structure

A

Sequence of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Secondary Structure

A

Amino acid chains with a more complex structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Tertiary Structure

A

Complex folding of polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Quaternary Structure

A

2+ polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Simple vs Conjugated Proteins

A

Conjugated proteins have a non-amino chemical associated with them, Simple proteins don’t

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

215nm

A

Peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

280nm

A

Aromatic rings in amino acids
Tyrosine
Tryptophan
Phenylalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Biuret reagent

A

Copper sulfate + NaOH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Do amino acids and dipeptides react with biuret? Why or why not?

A

No, require at least TWO peptide BONDS.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What interferants can interfere with biuret measurement?

A

Hemolysis and icterus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Biuret color change in the presence of protein

A

Blue to Violet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Total serum protein amount

A

6-8 g/dL

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Biuret cannot be used with what specimen?

A

Urine, CSF

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Biuret is insensitive for what kinds of proteins?

A

Globulins and other proteins that aren’t albumin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

When would biuret’s insensitivity to other proteins be an issue?

A

When multiple myeloma present

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Albumin measurement

A

Bromcresol green
Bromcresol purple

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What % of plasma protein is albumin?

A

50%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Globulins definition

A

All plasma proteins NOT albumin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

TP formula

A

Albumin + Globulins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Globulins calculation

A

Total protein - Albumin = Globulins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

A/G Ratio

A

Albumin / Globulins

22
Q

Albumins reference intervals

A

3.5-5 g/dL

23
Q

Globulins reference intervals

A

2.5-3 g/dL

24
Q

Urine protein reference intervals

A

1-14 mg/dL
or
< 100 mg/24hr

25
Q

CSF Protein reference intervals

A

15-45 mg/dL

26
Q

Buffer of Electrophoresis pH; why is it that?

A

8.6, Alb & Globs net negative charge so they will move to their isoelectric points

27
Q

Which protein has the biggest net negative charge and thus moves fastest?

A

Albumins

28
Q

Formula for urine total protein measurement per 24 hours

A

look it up

29
Q

Anode

A

Positive pole; Anions move towards it

30
Q

Cathode

A

Negative pole; Cations move towards it

31
Q

Heavy application point can be caused by

A

Thawed specimen with precipitated protein on it

32
Q

Which end of the medium is the application point?

A

Towards the cathode end (negative end)

33
Q

Lowest net negative charge

A

Globulins

34
Q

Highest net negative charge

A

Albumin

35
Q

Most anodal band

A

Albumin, the fastest

36
Q

Most cathodal band

A

Globulins, the slowest

37
Q

Frictional Coefficient: Larger pores

A

Separation based on size AND charge
Larger and more complex molecules move slower

37
Q

Frictional Coefficient: Smaller pores

A

Separation based on charge only

38
Q

What Is the electrolyte present in the medium that is required for electrons to flow through the medium?

A

Sodium barbital

39
Q

Support Media and their uses

A

Paper - Historic & Awful
Cellulose Acetate - Historic
Agarose - Common, separation based on charge
Polyacrylamide - Specialized, separation based on charge and size

40
Q

What causes smile gel

A

Temperature

41
Q

Wick flow

A

Evaporation, proteins make a trail

42
Q

How is wick flow fixed

A

Keep a lid on
Cool the system
Change buffer often/use fresh buffer

43
Q

Electroendosmosis

A

Cations bump into anions like gamma globulins as they move towards the cathode and cause the gamma globulins to move backwards

44
Q

Why does the albumin band look fat

A

Tracer dyes bind to a portion of the albumin

45
Q

Two albumin bands can be due to

A

Drugs that bind to albumin
or
Genetic bisalbuminemia

46
Q

Complement band on SPEP

A

In fresh specimen
Faint line in second Beta region

47
Q

Fibrinogen band

A

Plasma or specimen that didn’t clot
Between beta and gamma (after second band)

48
Q

How to fix fibrinogen band

A

Add thrombin so that specimen clots

49
Q

What does hemolysis do to SPEP

A

Joins alpha-2 and beta bands

50
Q

Where is CRP seen on SPEP?

A

Gamma region near application point

51
Q

Serum proteins are produced where?

A

Mostly in the liver, but not the antibodies