Alpha protoxin of StaphyZococcus 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 aminoacid analyses of activated toxin suggested that leucine or isoleucine is the N-terminus, in contrast to protoxin, the N-terminus of which is histidine.
DodgeJ. T.,
MitchellC.,
HanahanD. J.1963; The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Archs Biochem. Biophys 100:119
Fraenkel-ConratH.,
HarrisJ. I.,
LevyA. L.1955; Recent developments in techniques for terminal and sequence studies in peptides and proteins. Meth. biochem. Anal 2:359
FreerJ. H.,
ArbuthnottJ. P.,
BillcliffeB.1973; Effects of staphylococcal alpha toxin on the structure of erythrocyte membranes: a biochemical and freeze-etching study. J. gen. Microbiol 75:321
RobinsonJ.,
ThatcherF. S.,
MontfordJ.1960; Studies with staphylococcal toxins. V. Possible identification of alpha hemolysin with a proteolytic enzyme. Can. J. Microbiol 6:183
WisemanG. M.,
CairoJ. D.1972; Further observations on the mode of action of the alpha toxin of Staphylococcus aureus “Wood 46”. Can. J. Microbiol 18:987
WittlerR. G.,
PillemerL.1948; The immunochemistry of toxins and toxoids. V. The solubility of staphylococcal toxin in methanol-water mixtures under controlled conditions of pH, ionic strength and temperature. J. biol. Chem 174:23