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.

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/content/journal/micro/10.1099/00221287-123-2-223
1981-04-01
2021-08-01
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