Liberation of surface-located penicillinase from Staphylococcus aureus
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چکیده
منابع مشابه
Liberation of surface-located penicillinase from Staphylococcus aureus.
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 ...
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The isolation of mutants of Staphylococcus aureus that are affected in the stability of penicillinase plasmids is described. One mutation is plasmid borne and results in nonreplication of the plasmid at 42 C. A second type of mutation is host-borne and gives rise to instability of both mcr(I) and mcr(II) penicillinase plasmids but not a tetracycline-resistant plasmid.
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Growth of Stapylococcus aureus in various ionic surface-active agents resulted in loss of the ability to produce penicillinase, whereas growth in nonionic surface-active agents had no effect on penicillinase production. The curing effect of various alkyl sulfates was found to be dependent upon the chain length. Curing by surface-active agents could be inhibited by magnesium. Reciprocal transduc...
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A series of plasmids harbored by naturally occurring penicillin-resistant strains of Staphylococcus aureus were surveyed with a view toward exploring the variability in plasmid-linked marker patterns. Plasmids were transduced from their natural hosts to either of two plasmid-negative laboratory strains by selection for cadmium resistance, and the transductants were tested for all other markers ...
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The effects of various factors on the release of penicillinase from apparently undamaged cells of a growing culture of Bacillus subtilis were investigated. The enzyme was not eluted from the cells by treating them with high concentrations of salt. Its liberation did not take place at all a t Oo, and was nearly completely inhibited a t pH values below 6.0, whereas chloramphenicol, at concentrati...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1967
ISSN: 0006-2936
DOI: 10.1042/bj1020742