1887

Abstract

It was established that grew rapidly in a simple medium containing yeast extract (0·2 %, w/v) plus glucose (2 %, w/v). These cultures were in or near to a state of nitrogen limitation and the concentration of secreted aspartate proteinase increased rapidly (within 3–4 h) on addition of BSA. Synthesis and secretion were apparently controlled both positively (induction by albumin or, more probably, the peptides produced from it) and negatively (repression by NHCl). A small intracellular pool of the enzyme was detected during production of the enzyme and this pool decreased with the cessation of synthesis and secretion. A stable mutant, IR24, was isolated which secreted less than 0·3% of the amount of the proteinase exported by the parent strain ATCC 10261. The LD values for mutant IR24 and the parent strain administered intravenously to mice were > 1·0 × 10 and 1·6 × 10 c.f.u. kg respectively.

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1990-04-01
2024-04-26
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