Masters Theses

Abstract

"The enzyme indole acetic acid oxidase is produced by the fungus Hygrophorous conicus when it is grown in the presence of indole acetic acid (IAA) or tryptamine. The IAA acts both as an inducer and a substrate for this intracellular enzyme. The product of the oxidation catalyzed by the IAA oxidase is oxindole acetic acid (OIAA).

The rate of growth and the rate of formation of the enzyme IAA oxidase by H.conicus were studied in different media. Of these, a nitrate medium containing 0.5 per cent Yeast extract (Y.E.) was found to be the best for the production of H.conicus mycelium. A maltose medium was better than the other media tested so far as the growth of H,conicus and the formation of the enzyme IAA oxidase were concerned, The addition of 0.5 per cent Y.E. to any of the media tested suppressed the formation of the enzyme IAA oxidase of H.conicus.

The Krebs cycle enzyme succinic dehydrogenase was found in the particulate fraction, sedimented at 24,000 x g for 20 minutes from a cell-free preparation of H,conicus.

The use of sonic oscillations for 10 minutes at 4-5⁰C was found to solubilize, to some extent, the enzyme succinic dehydro genase of H,conicus.

The phenazine methosulfate method for the assay of succinic dehydrogenase activity gave higher QO₂(N) values than the cytochrome c method"--Abstract, pages ii-iii.

Advisor(s)

Siehr, Donald J.

Committee Member(s)

Grigoropoulos, Sotirios G.
Kincannon, Donny F.
Hanna, Samir B.

Department(s)

Chemistry

Degree Name

M.S. in Chemistry

Publisher

University of Missouri at Rolla

Publication Date

1966

Pagination

viii, 90 pages

Note about bibliography

Includes bibliographical references (pages 67-70).

Rights

© 1966 Jagdish M. Mehta, All rights reserved.

Document Type

Thesis - Open Access

File Type

text

Language

English

Library of Congress Subject Headings

Succinate dehydrogenase
Indoleacetic acid
Krebs cycle
Mitochondria
Oxidases

Thesis Number

T 1841

Print OCLC #

5972964

Electronic OCLC #

896725639

Included in

Chemistry Commons

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