In the given experiment, the observation needs to be explained, if the given protein does not contain any disulfide bond and if it contains a single disulfide bond. An experiment to identify the cysteine residue containing the disulfide bond needs to be explained. Concept introduction: 2-D electrophoresis is a technique that is used to analyze proteins. Here mixture of proteins is separated based on two properties in two dimensions of the same gel. Normally, in the first dimension proteins are separated according to the isoelectric point and then the proteins are separated in a perpendicular dimension based on their mass.

Question

The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S = Catalytic efficiency with T = Catalytic efficiency with U = Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?

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Question

Chapter 3, Problem 28P

Interpretation Introduction

Interpretation:

In the given experiment, the observation needs to be explained, if the given protein does not contain any disulfide bond and if it contains a single disulfide bond. An experiment to identify the cysteine residue containing the disulfide bond needs to be explained.

Concept introduction:

2-D electrophoresis is a technique that is used to analyze proteins. Here mixture of proteins is separated based on two properties in two dimensions of the same gel. Normally, in the first dimension proteins are separated according to the isoelectric point and then the proteins are separated in a perpendicular dimension based on their mass.

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