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Penicillinase activity can be reliably estimated iodometrically (Perret, 1954;Ghosh & Borkar, 1961), manometrically (Henry & Housewright, 1947), and alkalimetrically (Wise & Twigg, 1950), as well as by bio-assay (Pollock, 1956).However, staphylococcal penicillinase has so great an affinity for its substrate (Novick, 1962) that only the bio-assay is sensitive at the low substrate con- centrations necessary for the study of enzyme kinetics.The bio-assay has been used successfully for the estimation of the Michaelis constant (Kin) of Bacillu8 cereus penicillinase (Pollock, 1956), but it is unwieldly and time-consuming and is unsuitable for the precise measurement of initial reaction velocities because, to be reliable, any single measurement must be based on the destruction of at least one-quarter of the substrate initially present.
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Richard P. Novick (1962) studied this question.
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