1887

Abstract

SUMMARY: NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42) from ATCC 354 was purified to homogeneity by ammonium sulphate fractionation, followed by DEAE cellulose and Sephadex G-200 chromatography. The pH optimum of the enzyme was 8·5. The values for isocitrate and NADP were 74 and 53 μ, respectively. Mn was essential for enzyme activity. The enzyme lost all activity on incubation at 70°C for 15 min; isocitrate and NADP protected against this thermal inactivation. -Chloromercuribenzoate inhibited the enzyme; pre-incubation of enzyme with isocitrate + Mn prevented this inhibition. The purified enzyme showed concerted inhibition by glyoxylate + oxaloacetate and was inhibited by oxalomalate.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-133-9-2457
1987-09-01
2019-10-18
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-133-9-2457
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