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 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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