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Liberation of surface-located penicillinase from Staphylococcus aureus.

ABSTRACT: 1. Growth of Staphylococcus aureus (8325; alphai(-)p(+)), constitutive for the production of penicillinase, in CY medium results in about 40% of the enzyme being free in the medium. By modifying the medium, 98% of the enzyme remains cell-bound. 2. Part of this is bound ionically to the surface of the cell wall and may be liberated instantaneously by certain inorganic anions. Maximum liberation was achieved with either phosphate or arsenate, both of which showed marked pH-dependence. 3. Polyanions that do not penetrate the cell wall, such as heparin, RNA and dextran sulphate, are also effective in liberating penicillinase. 4. Polyanions added to the growth medium prevent the appearance of ionically bound penicillinase owing to their strong affinity for the sites on the cell wall required for binding of the enzyme.

SUBMITTER: Coles NW

PROVIDER: S-EPMC1270322 | biostudies-other | 1967 Mar

REPOSITORIES: biostudies-other

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Influence of organic anions on the liberation of penicillinase from Staphylococcus aureus.

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Monoclonal Antibody Targeting Staphylococcus aureus Surface Protein A (SasA) Protect Against Staphylococcus aureus Sepsis and Peritonitis in Mice.

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2024-02-09 | GSE249024 | GEO

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