[Isolation and properties of an extracellular proteinase of Staphylococcus aureus].
Serine proteinase splitting the peptide bonds which are formed by carboxyl groups of dicarboxylic amino acids was isolated from the supernatant of the Staphylococcus aureus culture liquid. It is similar to the enzyme isolated by Drapeau from Staphylococcus aureus strain V8 in its specifidity, molecular weight, amino acid composition, existence of two pH optima (pH 4.6 and 8.2). But there are some differences between the two proteinase in the content of dicarbonic amino acid residues. It was found that the enzyme can exist in two molecular forms.
D000596:Amino Acids / Q000032:analysis; D003470:Culture Media / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D020689:Exopeptidases; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification*; D011480:Protease Inhibitors; D013211:Staphylococcus aureus / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D003470:Culture Media; D011480:Protease Inhibitors; D020689:Exopeptidases; D010447:Peptide Hydrolases
Vydelenie i svoĭstva vnekletochnoĭ proteinazy zolotistogo stafilokokka.