Abstract
THE series of iodometric methods1 for assaying penicillinase reported here permits enzyme activity to be measured easily over wide ranges of pH and temperature, with higher speed, accuracy or sensitivity than were previously attainable2. Although designed for the penicillinase of B. cereus NRRL-569, it appears likely that they may be equally suitable in principle for penicillinase from other sources. ‘Unit rate of penicillin destruction’ is used here to mean a destruction-rate of 1 µmol./hr. Since the amount of a penicillinase which will give unit rate of destruction depends on the nature of the enzyme and the conditions to which it is exposed, a ‘unit dose’ (U.D.) of B. cereus NRRL-569 penicillinase is here defined as that amount of the enzyme which gives unit rate of destruction when exposed to 0.005 M sodium benzyl penicillin in 0.2 M potassium phosphate buffer at pH 6.5 and 30° C. The commercial crystalline sodium penicillin G of Glaxo, Ltd., is used in the following assays; its potency is stated to be 1,650 I.U./mgm.
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References
“The Chemistry of Penicillin”, 1026 (Princeton Univ. Press, Princeton, N.J., 1949).
“Antibiotics”, chapter 33 (Oxf. Univ. Press, London, 1949). “The Enzymes”, 1, chapter 37 (Academic Press, New York, 1951).
Peat, S., Bourne, E. J., and Thrower, R. D., Nature, 159, 810 (1947).
Manson, E. E. D., and Pollock, M. R., J. Gen. Microbiol., 8, 163 (1953).
Pollock, M. R., and Torriani, A.-M., C.R. Acad. Sci., Paris, 237, 276 (1953).
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PERRET, C. Iodometric Assay of Penicillinase. Nature 174, 1012–1013 (1954). https://doi.org/10.1038/1741012a0
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DOI: https://doi.org/10.1038/1741012a0
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