1887

Abstract

Two proteinases have been purified from mycelial extracts of Both enzymes have pH optima between 6·5 and 7·5 and are inhibited by phenylmethane sulphonyl fluoride and by di-isopropyl fluorophosphate. The molecular weights and isoelectric points of proteinase I and proteinase II are 30900 and 30000, and 4·6 and 4·3, respectively. Both enzymes have a similar range of substrate specificities. The principal differences in their properties are that proteinase I is sensitive to inhibition by 1 mM mercurials whereas proteinase II is not appreciably inhibited at this concentration, and that proteinase I is much more sensitive to denaturation by urea, guanidine hydrochloride and sodium dodecyl sulphate.

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/content/journal/micro/10.1099/00221287-129-6-1637
1983-06-01
2021-08-05
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