Purification of Yeast Proteinases

Part II. Purification and Some Properties of Yeast Proteinase C

Abstract

Yeast proteinase C which shows strong esterolytic activity against N-acetyl-L-tyrosine ethylester was successfully purified from baker's yeast. After repeated chromatography on TEAE-cellulose column, a single elution pattern was obtained regarding protein and the esterolytic activity. The proteolytic activity could not be measured in 0.5% casein solu-tion, but was observed clearly by the use of 4% casein solution as the substrate.
Both of the proteolytic activity and the esterolytic activity were inhibited by the sulf-hydryl reagents such as p-mercuribenzoate and also by diisopropylphosphorofluoridate.