Publication Date

1978

Document Type

Dissertation/Thesis

First Advisor

Erman, James E.

Degree Name

M.S. (Master of Science)

Legacy Department

Department of Chemistry

LCSH

Ascorbate; Reduction; Chemical; Cytochrome c

Abstract

The rate of reduction of cytochrome c̲ by ascorbate was examined as a function of binding to phospholipid vesicles (liposomes) of different compositions at low ionic strength. The binding of cytochrome c̲ to vesicles decreases the rate of reduction by ascorbate by a factor of up to 100. Increasing the concentration of phosphatidic acid in the vesicles increases the strength of the binding and therefore decreases the rate of reduction. These results can be primarily explained on electrostatic grounds. A simple method for measuring the cytochrome c̲-liposome binding equilibrium dissociation constant in a dynamic situation without disturbing the system is described, and values of the dissociation constant given for the different vesicle compositions. An appendix describes in detail unsuccessful attempts to isolate cytochrome c̲₁ from yeast using a combination of two procedures from the recent literature, and from detergent extracts of the water-insoluble debris remaining after separating out the water-soluble portion for the isolation of cytochrome c̲ peroxidase.

Comments

Includes bibliographical references.||Includes illustrations.

Extent

iv, 31 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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