These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: PURIFICATION OF STAPHYLOCOCCAL BETA-HEMOLYSIN AND ITS ACTION ON STAPHYLOCOCCAL AND STREPTOCOCCAL CELL WALLS.
    Author: CHESBRO WR, HEYDRICK FP, MARTINEAU R, PERKINS GN.
    Journal: J Bacteriol; 1965 Feb; 89(2):378-89. PubMed ID: 14255704.
    Abstract:
    Chesbro, William R. (University of New Hampshire, Durham), Fred P. Heydrick, Roland Martineau, and Gail N. Perkins. Purification of staphylococcal beta-hemolysin and its action on staphylococcal and streptococcal cell walls. J. Bacteriol. 89:378-389. 1965.-After growth of bovine-derived strains of Staphylococcus aureus in a completely dialyzable medium, the beta-hemolysin in the culture supernatant fluids was purified by gradient-elution chromatography on cellulose phosphate. The purified hemolysin contained two components, demonstrable by immunodiffusion or electrophoresis, but was free from alpha-hemolysin, coagulase, Delta-hemolysin, enterotoxins A and B, glucuronidase, hyaluronidase, lipase, muramidase, Panton-Valentine leukocidin, phosphatase, and protease. The hemolysin was heat-labile and sulfhydryl-dependent, and the preparation was leukocidal for guinea pig macrophages. When rabbit red blood cell (RBC) stroma and staphylococcal or enterococcal cell walls were treated with the purified hemolysin, it liberated mucopolysaccharides from the rabbit RBC stroma, polysaccharides and mucopolysaccharides (or mucopeptides) from the staphyloccoal cell walls, and rhamnose, glucose, an unidentified monosaccharide, N-acetylglucosamine, and at least two polysaccharides from the enterococcal cell walls. The hemolytic and cell-wall degradative activities had similar thermal inactivation kinetics, pH optima, sedimentation coefficients, and chromatographic and electrophoretic mobilities; both required Mg and were inhibited by thiol-inactivating agents. Consequently, it seems likely that both activities are expressions of the same enzyme.
    [Abstract] [Full Text] [Related] [New Search]