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- W2055883329 abstract "1. A β-lactamase of an Escherichia coli strain carrying an R factor derived from a Proteus strain, β-lactamase75, was purified as a single peak on Sephadex and a single band on disc electrophoresis. 2. The molecular weight as determined by gel filtration and by disc electrophoresis was coincident and was 26 000. 3. The isoelectric point determined by the electrofocusing method was 5.26. 4. β-Lactamase75 is quite sensitive to heat and is strongly inhibited by organic mercurials. In addition, the rate of hydrolysis of penicillin G and cephaloridine by this enzyme is greatly retarded by the presence of cloxacillin. From the results, it is concluded that β-lactamase75 is a new type of β-lactamase. 5. Preliminary amino acid analysis showed the presence of cysteine. The significance of the cysteine residue is discussed in relation to the active site of this enzyme." @default.
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- W2055883329 date "1972-11-01" @default.
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- W2055883329 title "A β-lactamase of Escherichia coli" @default.
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- W2055883329 doi "https://doi.org/10.1016/0005-2744(72)90123-4" @default.
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