Publication Date

1968

Document Type

Dissertation/Thesis

First Advisor

Lynch, Darrel L.

Degree Name

M.S. (Master of Science)

Department

Department of Biological Sciences

LCSH

Spores (Bacteria)||Glucose||Actinoplanes philippinensis||Spectrophotometry

Abstract

This study was designed to furnish evidence showing the possible pathways utilized by Actinoplanes philippinensis ATCC 11242 in the dissimilation of D-glucose. A. philippinensis was grown in a defined medium using D-glucose as its carbon source. Escherichia coli ATCC 9257h was cultivated under the same conditions and used for comparative purposes. Quantitative enzyme assays on cell free extracts were determined spectro-photometrically for glucokinase, glucose-6-phosphate dehydrogenase, phosphoglucoisomerase and 6-phosphogluconate dehydrogenase. Enzymic activities showed the presence of glucokinase, glucos-6-phosphate dehydrogenase and phosphoglucoisomerase in A. philippinensis. Six-phosphogluconate dehydrogenase on the basis of observed activity is either absent or may be present in very low concentrations in this species of Actinoplanes. If so, this substantially rules out the H.M.P. pathway for dissimilation of glucose by this bacterium. A qualitative test for aldolase indicated its presence in the organism. Possible pathways in D-glucose catabolism for A. philippinensis would appear to be either the Entner-Doudoroff, Embden-Meyerhof, or a modification of these pathways.

Comments

Bibliography: pages [28]-31.

Extent

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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