Open AccessTrypsin-Mediated Activation of the -Haemolysin of Staphylococcus Aureus
Author(s) -
G. M. Wiseman,
J. D. Caird,
Hugh B. Fackrell
Publication year - 1975
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-8-1-29
Subject(s) - trypsin , toxin , isoleucine , biochemistry , arginine , chemistry , staphylococcus aureus , microbiology and biotechnology , histidine , aminopeptidase , hemolysin , enzyme , leucine , amino acid , biology , bacteria , virulence , gene , genetics
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.