1887

Abstract

SUMMARY: Malate dehydrogenase (MDH; EC 1.1.1.37) from was purified and characterized. MDH activity from whole cells was purified 275-fold. The mitochondrial cytoplasmic MDH present co-purified through three ion exchange and affinity chromatography steps. The isoenzymes were barely separable by either disc gel electrophoresis or isoelectric focusing. The purified preparation containing both isoenzymes had a single pH optimum (9.3–9.5) and an apparent molecular weight of 70000. It exhibited linear kinetics and responded to known inhibitors of MDH, i.e. thyroxine and hydroxymalonate. Michaelis and dissociation constants obtained with this preparation were similar to those obtained with a 10-fold purified mitochondrial MDH.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-128-8-1767
1982-08-01
2020-01-21
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-128-8-1767
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error