1887

Abstract

Glyceraldehyde-3-phosphate dehydrogenase was purified from by sequential ammonium sulfate precipitation, gel filtration and anion-exchange chromatography (to a specific activity of 27 U mg). The enzyme had a molecular mass of 40 kDa as determined by SDS-PAGE and a native molecular mass of 160 kDa as determined by nondenaturing PAGE, indicating that it has a homotetrameric composition. Its pH optimum was between 8.5 and 9.3. The corresponding gene () was cloned and sequenced from DSM 792 and found to cluster with other genes of enzymes from the glycolytic pathway (, phosphoglycerate kinase; , triosephosphate isomerase; (i), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase). No sequences resembling rho-independent transcription terminators were found in the intergenic regions. A plasmid carrying the clostridial gene complemented an mutant.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-145-8-1839
1999-08-01
2019-10-18
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-145-8-1839
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