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MELS301 > Proteins Wk 2 > Flashcards

Proteins Wk 2 Flashcards

1
Q

What is the primary protein structure

A

Linear amino acid sequence
All have this

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2
Q

What is the secondary protein structure

A

Alpha helix, beta sheets and random coil

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3
Q

What is the tertiary protein structure

A

3D, globular and fibrous

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4
Q

What is the quaternary structure

A

Not all proteins have this
Multi protein assemblies

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5
Q

What are examples of extra functional prosthetic groups or ligands on proteins

A

VDL, HDL, transferrin, lipoproteins

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6
Q

What is the amino acid configuration of biological relevant ones

A

L configuration

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7
Q

What is a zwitterion

A

Dipolar
Depends on solution pH, most amino acids are in this form at physiological pH7.4

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8
Q

Are amino acids water soluble

A

Most are

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9
Q

How many proteins are in plasma

A

3500 types

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10
Q

Main functions of proteins

A

Transporting other molecules (Hb, transferrin)
Structural (collagen, keratin)
Regulatory WIRH enzymes
Hormonal (insulin)

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11
Q

What is the most abundant protein

A

Albumin
Maintains blood pressure in blood vessels

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12
Q

What is total protein

A

All the protein in plasma, heterogenous with different charges/physical characteristics

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13
Q

What is total protein measured? What is the method called

A

Biuret method
Spectrophotometry

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14
Q

What to consider when choosing analytical methods

A

Analyte size/charge/structure
How it interacts with light
Potential interferences
Do you want quantitative or qualitative
Tech available
Cost

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15
Q

What is spectroscopy

A

Study of how energy and matter interact

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16
Q

What is spectrometry

A

The practical application of spectroscopy

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17
Q

Spectrophotometry

A

The measurement of light spectra as presented as a wavelength

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18
Q

What does beer lambert law mean

A

Where linearity exists absorbance and concentration are directly proportional

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19
Q

Visible light is between what wavelength size

A

700nm -400 nm

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20
Q

What makes something appear a certain colour

A

If it absorbs the opposite colour

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21
Q

If the substance absorbs red what colour do you see

A

Blue-green

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22
Q

Total protein absorbs green light so you see

A

Purple

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23
Q

What is the chemistry behind the biuret method

A

Strong alkaline solutions have copper ions that form complexes with peptide bonds, this changes it’s wavelength causing a colour change from blue to purple

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24
Q

What wavelength was TP measured at

A

540nm

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25
Q

If you see purple in biuret reaction what does this mean in terms of the other colours

A

All colours except violet is absorbed by the sample and violet is reflected or red/blue/violet is reflected

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26
Q

What are some potential interferences for the biuret method

A

anything with an absorbance at 540nm
Haemolysis causes interference as Hb as a similar absorbance maxima and lots of proteins are released which also interfere

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27
Q

What does the buffer do in electrophoresis

A

Carries the current and controls the pH

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28
Q

Why is it important to regulate the buffer and so the pH

A

pH determines
The rate of migration, which electrode the solute migrates too, the sharpness of the zones, the electrical charge of the solute

29
Q

What is different between the capillary electrophoresis and gel

A

Capillary is automated and faster with better separation and higher voltage capacity on a much smaller sample size

30
Q

Is albumin negatively charged or positive

A

Negative, high peak at positive cathode as most abundant

31
Q

Where is albumin made

A

In the liver

32
Q

Half life of albumin

A

15-19 days

33
Q

Functions of albumin

A

Maintaining oncotic pressure
Transporter
Antioxidant activity

34
Q

How is albumin measured

A

Using dye binding as at low pH it will react with anionic dyes like green BCG and purple BCP

35
Q

What is albumin rich in

A

An anionic protein enriched in Asp and Glu

36
Q

Is binding for albumin specific using BCG or BCP

A

No because other proteins have Asp and Glu so read absorbance within 30s to increase specificity

37
Q

Can you measure albumin using binding dyes in any sample type

A

Yes you can use plasma/serum/urine

38
Q

BCG wavelength

A

630

39
Q

BCP wavelength

A

600nm

40
Q

Reasons for hyperalbuminemia

A

Dehydration
Tourniquet left on
Of no significance

41
Q

Reasons for hypoalbuminemia

A

Pregnancy dilutes it
Malignancy
Infection
Inflammation
Loss from kidney disease in urine
Loss from GI disease
Less production of albumin from liver failure, chronic inflammation and nutritional deficit

42
Q

What is seen in analbuminaemia

A

Edema
Low BP
Fatigue
Hypercholesterolemia
High LDL
Lower body lipidystrophy

43
Q

Bisalbuminaemia

A

2 types of albumin
Two peaks in electrophoresis
Rare - can be transient or inherited

44
Q

What proteins are found in the alpha 1 region of electrophoresis

A

Alpha 1 antitrypsin / fetoprotein/ acid glycoprotein

AAT
AFP

45
Q

What proteins are in the alpha 2 region

A

Haptoglobin
Cp
Macroglobulin

46
Q

When is Cp reduced

A

Wilson’s disease - excess Cu deposited in tissues and it’s role is to transport copper

47
Q

What is macroglobulin

A

A protease inhibitor
Largest non Ig protein in plasma
Inhibits thrombin

48
Q

When does macroglobulin is alpha 2 region increase

A

In nephrotic syndrome

49
Q

When do globulins increase

A

In inflammation, renal disease, and malignancy

50
Q

What is found in the beta protein region

A

Transferrin
Microglobulin BMG
C3 and C4 - complement

51
Q

When do complement proteins C3 and C4 decrease

A

Genetic deficiencies

52
Q

When do complement C3 and C4 increase

A

Inflammation

53
Q

Where is B2 Microglobulin found

A

In urine, small amounts as it’s small and can be filtered

54
Q

When is B2 Microglobulin increased

A

In renal failure - this can be filtered but should be reabsorbed
Inflammation
Neoplasia

55
Q

Gamma region proteins

A

CRP
Immunoglobulins

56
Q

When does CRP increase

A

Inflammation
Infection
Trauma

57
Q

How are immunoglobulins measured

A

Doing an immunoassay

58
Q

When do immunoglobulins increase

A

Malignancy - monoclonal gammopathy

Polyclonal hyperimmunoglobulinaemia

59
Q

Highly sensitive CRP increase =

A

Associated with increased CVD risk

60
Q

What are monoclonal immunoglobulins

A

Paraproteins

61
Q

What is an increase in Paraproteins associated with

A

Proliferation B cell disorders
As Paraproteins are free light chains which are made by plasma cells
Can be a plasma cell myeloma

62
Q

Where are free light chains found

A

In the urine in myeloma

63
Q

What is AFP and when is it screened

A

Alpha 1 fetoprotein
Screening in fetal abnormalities

64
Q

When is AFP elevated

A

Metastatic liver disease
Tumours in ovary and testis

65
Q

Where is A1 acid glycoprotein made

A

Liver
It is an acute phase protein

66
Q

How is alpha 1 antitrypsin measured

A

EP - screening
Immuniturbidimetry
Nephelometry

67
Q

When do you get a decrease in AAT

A

Pulmonary emphysema
Cirrhosis

68
Q

Where is AAT made

A

Liver
Inactivates trypsin

MELS301 (6 decks)

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