Secretion of staphylocoagulase be Staphylococcus aureus: the role of a cell-bound intermediate.

Antonie van Leeuwenhoek ·Vol. 47 ·No. 6 ·1981-00-00 ·Pages 509-24

Engels W, Kamps MA

Abstract

A cell-bound staphylocoagulase could be detected in chemostat cultures of Staphylococcus aureus 104 under magnesium-and oxygen-limited growth conditions. A distribution study revealed that 81% of the enzyme was membrane-bound and could be optimally released by Triton X-100. The remaining part was located in the periplasmic space and was released during protoplasting of organism. From inhibition studies with cerulenin, quinacrine, lincomycin an chloramphenicol, it was concluded that the cell-bound form was precursor in the secretion of extracellular staphylocoagulase. The involvement of a lipid intermediate/exoprotein-releasing protease system in the secretion of staphylocoagulase, and of exoproteins in general, is discussed.

MeSH Terms

Cell Membrane/enzymology Cerulenin/pharmacology Chloramphenicol/pharmacology Coagulase/metabolism Lincomycin/pharmacology Protoplasts/enzymology Quinacrine/pharmacology Sodium Chloride/pharmacology Staphylococcus aureus/drug effects,enzymology

Chemicals

Coagulase Cerulenin Sodium Chloride Chloramphenicol Lincomycin Quinacrine

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Engels W

Kamps M A

References (25)

25 references, click to expand

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Article Info

Journal

Antonie van Leeuwenhoek

Abbr.

Antonie Van Leeuwenhoek

ISSN

0003-6072

DOI

10.1007/BF00443238

Published

1981-00-00

Pages

509-24

Language

English

Region

Netherlands

NLM ID

0372625

Subset

External Links

PubMed source DOI: 10.1007/BF00443238 View journal details

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Secretion of staphylocoagulase be Staphylococcus aureus: the role of a cell-bound intermediate.

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