Off-campus South Dakota State University users: To download campus access theses, please use the following link to log into our proxy server with your South Dakota State University ID and password.

Non-South Dakota State University users: Please talk to your librarian about requesting this thesis through interlibrary loan.

Document Type

Thesis - University Access Only

Award Date

1990

Degree Name

Master of Science (MS)

Department / School

Biology and Microbiology

First Advisor

Helen N. Westfall

Abstract

Although enzymes catalyzing the reduction of nitrate to nitrite have been studied in a variety of organisms, very few of them have been suffiently [sic] purified to permit detailed characterization. The nitrate reductase enzymes of C. sputorum ssp. bubulus and C. fetus ssp. fetus have been partially purified in the present research. One basic premise of this research was that the nitrate reductase activity of C. fetus ssp. fetus would be similar to that of C. sputorum ssp. bubulus. Some research has been done on the nitrate reduction abilities of C. sputorum ssp. bubulus (42,53,62,77). Within the genus Campylobacter only C. sputorum ssp. bubulus and C. fetus ssp. fetus are able to degrade nitrate under anaerobic conditions. The potential for similarity of the enzymes was thought to be great. The results of this research indicated that the nitrate reductase activity of the two different species of Campylobacter is indeed similar.

Library of Congress Subject Headings

Campylobacter fetus
Campylobacter
Denitrifying bacteria

Format

application/pdf

Number of Pages

90

Publisher

South Dakota State University

Share

COinS