1887

Abstract

Proteolytic activity in a batch culture of R8/4 was maximal and largely (>90%) cell-associated during the mid-exponential phase of growth. The cell-bound protease was not inactivated during storage at −70 °C, was not significantly affected by pH over the range 5.9 to 8.2, but was subject to substrate inhibition by Fraction 1 protein (ribulose-1,5-bisphosphate carboxylase; EC 4.1.1.39) and was most active in the presence of thiol reagents. Radioactive Fraction 1 protein was hydrolysed by non-growing and growing cells of R8/4 with the production of peptides and free amino acids. Deaminase activity was absent. Radioactive amino acids were incorporated into bacterial proteins from [C]Fraction 1 protein without substantial change in specific radioactivity.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-123-2-223
1981-04-01
2019-12-14
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-123-2-223
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