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Chapter 5: Q5_2CP (page 109)

Describe how a protein may be quantified by an assay or by absorbance spectroscopy.

Short Answer

Expert verified

A protein may be quantified by observing the rate of product formation by coupled enzyme assay, radioimmunoassay (RIA), and enzyme-linked immunosorbent assay (ELISA).

Step by step solution

01

Coupled enzyme assay

In this reaction, the product of the first reaction is the substrate for the second. The determination of a substrate or enzyme activity by coupling one enzymatic reaction with another.

02

Radioimmunoassay (RIA)

It uses radiolabel molecules and is a very sensitive technique used to measure the concentration of antigens. e.g.(hormone levels in the blood through an antibody directed against these antigens).

03

Enzyme-linked immunosorbent assay (ELISA)

ELISA is used to detect antibodies in the blood. It involves 4 steps: Plate coating, Plate Blocking, Ab incubation, and Detection.

04

Absorbance spectroscopy

It works on the principle of Beer-Lambert law. It states that there is a linear relationship between the concentration and the absorbance of the solution.

A = 蓻cl

Where,

A = Absorbance

蓻= Molar absorption coefficient

c = Molar concentration

l = Optical path length

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Most popular questions from this chapter

Explain why a certain protein has an apparent molecular mass of 90kDwhen determined by gel filtration and 60kDwhen determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol. Which molecular mass determination is more accurate?

What fractionation procedure could be used to purify protein 1 from a mixture of three proteins whose amino acid compositions are as follows?

1. 25% Ala, 20% Gly, 20% Ser, 10% Ile, 10% Val, 5% Asn, 5% Gln, 5% Pro

2. 30% Gln, 25% Glu, 20% Lys, 15% Ser, 10% Cys

3. 25% Asn, 20% Gly, 20% Asp, 20% Ser, 10% Lys, 5% Tyr

All three proteins are similar in size and pI, and there is no antibody available for protein 1.

You wish to sequence the light chain of a protease inhibitor from the Brassica nigra plant. Cleavage of the light chain by trypsin and chymotrypsin yields the following fragments. What is the sequence of the light chain?

Chymotrypsin

1. Leu鈥揌is鈥揕ys鈥揋ln鈥揂la鈥揂sn鈥揋ln鈥揝er鈥揋ly鈥揋ly鈥揋ly鈥揚ro鈥揝er

2. Gln鈥揋ln鈥揂la鈥揋ln鈥揌is鈥揕eu鈥揂rg鈥揂la鈥揅ys鈥揋ln鈥揋ln鈥揟rp

3. Arg鈥揑le鈥揚ro鈥揕ys鈥揅ys鈥揂rg鈥揕ys鈥揚he

Trypsin

4. Arg

5. Ala鈥揅ys鈥揋ln鈥揋ln鈥揟rp鈥揕eu鈥揌is鈥揕ys

6. Cys鈥揂rg

7. Gln鈥揂la鈥揂sn鈥揋ln鈥揝er鈥揋ly鈥揋ly鈥揋ly鈥揚ro鈥揝er

8. Phe鈥揋ln鈥揋ln鈥揂la鈥揋ln鈥揌is鈥揕eu鈥揂rg

9. Ile鈥揚ro鈥揕ys

10. Lys

You wish to determine the sequence of a polypeptide that has the following amino acid composition.

1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1 Gln 4 Glu 1 His 1 Lys 1 Met 1 Phe 2 Pro 4 Ser 2 Tyr 1 Trp

(a) What is the maximum number of peptides you can expect if you cleave the polypeptide with cyanogen bromide?

(b) What is the maximum number of peptides you can expect if you cleave the polypeptide with chymotrypsin?

(c) Analysis of the intact polypeptide reveals that there are no free sulfhydryl groups. How many disulfide bonds are likely to be present?

(d) How many different arrangements of disulfide bonds are possible?

Protein X has an absorptivity of 0.4mL 路 mg-1路 cm-1 at 280nm. What is the absorbance at 280nm of a 2.0 mg 路 mL-1solution of protein X? (Assume the light path is 1cm.)
See all solutions

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