1887

Abstract

Glutamate dehydrogenase (-glutamate: NAD oxidoreductase (deaminating); EC 1.4.1.2) has been purified from in a single step using dye-ligand chromatography. The enzyme (GDH) was present in high yields and was stabilized in crude extracts. A subunit molecular weight of 49000 ± 500 was determined by SDS polyacrylamide gel electrophoresis and six bands were obtained after cross-linking the subunits with dimethyl suberimidate. This bacterial GDH was predominantly NAD-linked, but was able to utilize both NADP and NADPH at 4% of the rates with NAD and NADH, respectively. An investigation of the amino acid specificity revealed some similarities with GDH from mammalian sources and some clear differences. The values of apparent for the substrates ammonia, 2-oxoglutarate, NADH, NAD and glutamate were 18.4, 0.82, 0.066, 0.031 and 6 m, respectively. The GDH was not regulated by purine nucleotides, but was subject to strong inhibition with increasing ionic strength.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-130-9-2385
1984-09-01
2019-10-15
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-130-9-2385
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