Key points are not available for this paper at this time.
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.
Drapeau et al. (1972) studied this question.