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

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.

journal_name

J Med Microbiol

authors

Wiseman GM,Caird JD,Fackrell HB

doi

10.1099/00222615-8-1-29

keywords:

subject

Has Abstract

pub_date

1975-02-01 00:00:00

pages

29-38

issue

1

eissn

0022-2615

issn

1473-5644

journal_volume

8

pub_type

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