Work

Purification and Properties of an Extracellular Protease of Staphylococcus aureus

Year: 1972

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)44749-2

Authors: Gabriel R. Drapeau, Yves Boily, Jean Houmard

Institution: Université de Montréal

Language: English

Topic: Enzyme Production and Characterization

Subfield: Biotechnology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1594796409

FWCI: 10.99

Cites: 21

Cited by: 511

Related to: 10