This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Burton, S. D. Articles by Morita, R. Y. Search for Related Content PubMed PubMed Citation Articles by Burton, S. D. Articles by Morita, R. Y.

 Previous Article  |  Next Article 

J Bacteriol. 1963 November; 86(5): 1019-1024
Copyright © 1963, The Williams & Wilkins Company. All Rights Reserved.

DENATURATION AND RENATURATION OF MALIC DEHYDROGENASE IN A CELL-FREE EXTRACT FROM A MARINE PSYCHROPHILE¹

Departments of Microbiology and Oceanography, Oregon State University, Corvallis, Oregon

ABSTRACT

BURTON, SHERIL D. (Oregon State University, Corvallis), AND RICHARD Y. MORITA. Denaturation and renaturation of malic dehydrogenase in a cell-free extract from a marine psychrophile. J. Bacteriol. 86:1019–1024. 1963.—Malic dehydrogenase from a marine psychrophilic vibrio (PS 207) was found to be heat-sensitive at 30 C, the maximal growth temperature for the organism. Initial denaturation was reversible, with maximal renaturation occurring when the denatured enzyme was slowly cooled in the presence of mercaptoethanol, reduced nicotinamide adenine dinucleotide, and malate. No renaturation occurred when these compounds were added after slow cooling, or when the renaturation mixture was rapidly cooled. Mercaptoethylamine, cysteine, glutathione, or mercaptoacetic acid could not replace mercaptoethanol. The kinetics of denaturation and renaturation suggest the presence of several malic isozymes each with different heat labilities, or that these processes are occurring in several distinct steps.

¹ Published as technical paper no. 1689, Oregon Agricultural Experiment Station.