Purification and Properties of an Extracellular Protease of Staphylococcus aureus

Abstract

In this report a procedure for the purification of an extracellular protease of S. aureus, strain V8, is described and some of the characteristics of the purified enzyme such as 111-T optima, molecular weight, arnino acid composition, and substrate specificity are presented.This protease was sl~ow~l to cleave sl>ecifically the peptide bonds at the carbosyl-terminal side of either aspartic acid or glutarnic acid.