ElectrophoresisMacmillan LearningChymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with asingle band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin andlane 2 contains chymotrypsin pre-treated with performic acid.12Why does performic acid treatment of chymotrypsin generate three bands in lane 2?°Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues.The three peptides are impurities in the original chymotrypsin sample.Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues.Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin.Correct Answer

Chymotrypsin is a type of protease, which means it is an enzyme that helps break down proteins by…

Answered: Electrophoresis Macmillan Learning…

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.1: Introduction To Clinical Chemistry

Problem 9RQ

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Pathogenic E. coil have recently been shown to degrade tight junction proteins during infection. How would this provide an advantage to the bacteria?
Both of the regular intravenous solutions administered in medicine, normal saline and lactated Ringer’s solution, are isotonic. Why is this important?
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.
a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
Aquaporins are proteins embedded in the plasma membrane that allow water molecules to move between the extracellular matrix and the intracellular space. Based on its function and location, describe the key features of the protein’s shape and the chemical characteristics of its amino acids.
Cholesterol is an integral part of plasma membranes. Based on its structure, where is it found in the membrane? on the extracellular surface embedded with the phospholipid heads within the tail bilayer attached to the intracellular surface
Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
The synthetic process by which monomers are covalently linked is (a) hydrolysis (b) isomerization (c) condensation (d) glycosidic linkage (e) ester linkage
Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated? They are polar. They are non-polar. They contain a hydroxyl group. They occur more frequently in the amino acid sequence of signaling proteins.
Describe the differences in the four protein structures.

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