Open AccessCharacterization of staphylococcal -lysin
Author(s) -
Marguerite Clyne,
T. H. Birkbeck,
J. P. Arbuthnott
Publication year - 1992
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - Uncategorized
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-138-5-923
Subject(s) - haemolysis , lysin , papain , molecular mass , protease , trypsin , lysis , microbiology and biotechnology , gamma globulin , lysozyme , agarose , biochemistry , chemistry , hemolysis , enzyme , biology , immunology , bacteriophage , escherichia coli , antibody , gene
gamma-Lysin was purified from Staphylococcus aureus strains Smith 5R and PG23 (a toxic shock syndrome isolate) by a combination of heparin-agarose and hydroxylapatite chromatography. Both strains produced two haemolytic components, designated gamma 1 and gamma 2. Though each component was weakly haemolytic they acted synergistically to potentiate haemolysis on rabbit, sheep and human blood. Rabbit and sheep erythrocytes were more sensitive to lysis by gamma-lysin than human erythrocytes. The molecular mass of gamma 1 was 32 kDa and its pI value was 9.4. gamma 2 had a molecular mass of 36 kDa and a pI value of 9.3. While both trypsin and papain acted synergistically with gamma 2 to induce increased haemolysis, no such synergism was seen with gamma 1. Also, protease inhibitors acted to inhibit synergism between gamma 1 and gamma 2. These findings suggest that gamma 1 could be a protease.