Date of Award

1990

Document Type

Thesis

Degree Name

Master of Science

School

College of Arts and Sciences

Program

Biology MS

First Advisor

Ralph Scorpio

Second Advisor

John F. Stout

Third Advisor

Patricia Mutch

Abstract

In partially purified cell-free extracts of rat liver, nonexhaustive, daily exercise results in a 40 to 90% inhibition of FAB by decreasing the catalytic activity of acetyl coenzyme A carboxylase (ACC), the rate-limiting enzyme in the de novo FAB pathway in vitro. ACC inhibitory mechanisms are postulated to include: phosphorylation of ACC and production of a noncompetitive inhibitory substance.

Data obtained after purification of rat liver ACC to homogeneity suggest that decreased ACC activity in exercised rats cannot be attributed to the well-documented control of ACC by reversible phosphorylation, but are more likely due to the presence of a noncompetitive inhibitory substance located in the partially purified cell-free extract of rat liver.

Subject Area

Fatty acids, Rats--Exercise

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Biology Commons

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