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PMID: 1127680 Published · ppublish English Journal Article

Trypsin-mediated activation of the alpha-haemolysin of Staphylococcus aureus.

Journal of medical microbiology ·Vol. 8 ·No. 1 ·1975-02-00 ·Pages 29-38

Wiseman GM, Caird JD, Fackrell HB

Abstract

Alpha protoxin of Staphylococcus aureus "Wood 46" was activated by trypsin which had been coupled to carboxymethylcellulose, as indicated by the toxin's ability to hydrolyse tosyl-arginine methylester (TAME). A Lineweaver-Burk plot of the degradation of TAME by toxin and trypsin showed that toxin had a greater affinity for the substrate than had trypsin. N-terminal amino-acid analyses of activated toxin suggested that leucine or isoleucine is the N-terminus, in contrast to protoxin, the N-terminus of which is histidine.

MeSH Terms
Amino Acid Sequence Ammonium Sulfate Chemical Precipitation Chromatography, DEAE-Cellulose Chromatography, Gel Hemolysin Proteins/analysis,metabolism Hemolysis Histidine/analysis Hydrolysis Isoleucine/analysis Leucine/analysis Methanol Staphylococcus/immunology Tosyl Compounds/metabolism Trypsin/pharmacology
Chemicals
Hemolysin Proteins Tosyl Compounds Isoleucine Histidine Trypsin Leucine Ammonium Sulfate Methanol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wiseman G M
Caird J D
Fackrell H B
Article Info
Journal
Journal of medical microbiology
Abbr.
J Med Microbiol
ISSN
0022-2615
Published
1975-02-00
Pages
29-38
Language
English
Region
England
NLM ID
0224131
Subset
IM
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