Campbell Biology: Concepts & Connections, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (8th Edition)
Campbell Biology: Concepts & Connections, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (8th Edition)
8th Edition
ISBN: 9780133909029
Author: Jane B. Reece, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, Kelly A. Hogan
Publisher: PEARSON
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Chapter 5, Problem 15TYK

A biologist performed two series of experiments on lactase, the enzyme that hydrolyzes lactose to glucose and galactose. First, she made up 10% lactose solutions containing different concentrations of enzyme and measured the rate at which galactose was produced (grams of galactose per minute). Results of these experiments are shown in Table A below. In the second series of experiments (Table B), she prepared 2% enzyme solutions containing different concentrations of lactose and again measured the rate of galactose production.

Table A Reaction Rate and Enzyme Concentration

Chapter 5, Problem 15TYK, A biologist performed two series of experiments on lactase, the enzyme that hydrolyzes lactose to , example  1

Table B Reaction Rate and Substrate Concentration

Chapter 5, Problem 15TYK, A biologist performed two series of experiments on lactase, the enzyme that hydrolyzes lactose to , example  2

a. Graph and explain the relationship between the reaction rate and the enzyme concentration.

b. Graph and explain the relationship between the reaction rate and the substrate concentration. How and why did the results of the two experiments differ?

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A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License