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A sensitive enzymic assay for benzylpenicillin
Author(s) -
Baker W.L.
Publication year - 1985
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1985.tb03329.x
Subject(s) - benzylpenicillin , chemistry , microbiology and biotechnology , chromatography , biology , antibiotics , penicillin
A method has been developed for the determination of sodium benzylpenicillin concentrations in the range 3·3–33 μg/ml. 6‐Aminopenicillanic acid is released from the benzylpenicillin by the action of the enzyme penicillin acylase and is estimated from its reaction with fluorescamine at pH 4.7‐Aminocephalosporanic acid shows a similar trend to 6‐aminopenicillanic acid in its reaction at pH 4. The open β‐lactam ring form of each compound shows little fluorescence with fluorescamine at pH but shows strong fluorescence in the pH range 7–9. 6‐Aminopenicillanic acid and its open β‐lactam ring form give different fluorescent responses to increasing volumes of a solution of the fluorigenic agent at pH 7·8. This effect can be used to estimate concentrations in a mixture of the two components providing other amino material is absent.