1887

Abstract

Intracellular and extracellular samples from the extremely thermophilic archaeobacterium showed the presence of multiple active proteinases. Using gelatin-containing SDS-PAGE, up to 13 activity bands were visualized with apparent molecular masses of between 66 and 135 kDa. Characterization studies revealed these bands to be due to discrete polypeptides, and not artefacts. Results from gel permeation chromatography, sucrose density gradient centrifugation and non-denaturing PAGE suggested that some of these proteohtic polypeptides may exist as active aggregates either or before being dissociated by SDS to active monomers.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-137-5-1193
1991-05-01
2019-11-17
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-137-5-1193
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