Two structurally different NADP-specific isocitrate dehydrogenases in an obligately psychrophilic bacterium, Vibrio sp. strain ABE-1.
- 1 January 1984
- journal article
- research article
- Published by Microbiology Research Foundation in The Journal of General and Applied Microbiology
- Vol. 30 (6) , 479-487
- https://doi.org/10.2323/jgam.30.479
Abstract
Two isozymes of NADP-specific isocitrate dehydrogenase (EC 1.1.1.42) were purified from the obligately psychrophilic marine bacterium Vibrio sp. strain ABE-1. Isozyme I purified by Blue-Sepharose column chromatography was proved to consist of 2 subunits by sodium dodecyl sulfate polyacrylamide gel electrophoresis and cross-linking with dimethyl suberimidate. Isozyme II purified by NADP-Sepharose column chromatography was a single large polypeptide. This extremely thermolabile isozyme was easily inactivated above 15.degree. C and reactivated by chilling at 0.degree. C in the presence of 2-mercaptoethanol. Even when inactivated completely at 40.degree. C it could be renatured to .apprx. 40% of the original activity under the appropriate conditions. Isozyme I once denatured could not be renatured.This publication has 0 references indexed in Scilit: