title: 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.
mesh_terms: D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D006460:Hemolysin Proteins / Q000032:analysis / Q000378:metabolism*; D006461:Hemolysis; D006639:Histidine / Q000032:analysis; D006868:Hydrolysis; D007532:Isoleucine / Q000032:analysis; D007930:Leucine / Q000032:analysis; D000432:Methanol; D013210:Staphylococcus / Q000276:immunology*; D014105:Tosyl Compounds / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology*
chemical_list: D006460:Hemolysin Proteins; D014105:Tosyl Compounds; D007532:Isoleucine; D006639:Histidine; D014357:Trypsin; D007930:Leucine; D000645:Ammonium Sulfate; D000432:Methanol