The purification and properties of two staphylolytic enzymes from Streptomyces griseus.

The Biochemical journal ·Vol. 106 ·No. 1 ·1968-01-00 ·Pages 69-76

Ward JB, Perkins HR

Abstract

1. Two staphylolytic enzymes have been purified from cultures of a soil isolate of Streptomyces griseus. 2. The purified enzymes were shown to be basic proteins of low molecular weight. Each enzyme released N-acetylmuramic acid reducing groups from the cell walls of Staphylococcus aureus. 3. The enzymes lysed whole staphylococci best at higher pH values and lower ionic strengths than when the substrate was isolated cell walls or purified mucopeptide. 4. Added teichoic acid did not inhibit the enzymes, but it formed an ethanol-precipitable complex with them. 5. The possibility that teichoic acid on the surface of whole cells prevents the access of the enzymes to their mucopeptide substrate is discussed.

MeSH Terms

Bacterial Proteins/isolation & purification Bacteriolysis Buffers Cell Wall Enzyme Inhibitors Enzymes/isolation & purification Hydrogen-Ion Concentration Molecular Weight Mucoproteins Osmolar Concentration Pentosephosphates Peptides Ribose Staphylococcus Streptomyces/enzymology Time Factors

Chemicals

Bacterial Proteins Buffers Enzyme Inhibitors Enzymes Mucoproteins Pentosephosphates Peptides Ribose

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Ward J B

Perkins H R

References (28)

28 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1060069

Published

1968-01-00

Pages

69-76

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1198470

Subset

External Links

PubMed source DOI: 10.1042/bj1060069 PMC Full Text View journal details

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The purification and properties of two staphylolytic enzymes from Streptomyces griseus.

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