@article{mbs:/content/journal/jmm/10.1099/00222615-8-1-29, author = "Wiseman, G. M. and Caird, J. D. and Fackrell, H. B.", title = "Trypsin-Mediated Activation of the α-Haemolysin of Staphylococcus Aureus", journal= "Journal of Medical Microbiology", year = "1975", volume = "8", number = "1", pages = "29-38", doi = "https://doi.org/10.1099/00222615-8-1-29", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/00222615-8-1-29", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", abstract = "SUMMARY 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.", }