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Ester-hydrolysing Activity of Urokinase Preparations

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Abstract

NITROPHENYL esters have proved to be very useful in examining hydrolytic enzymes1,2. The usually rapid rate of hydrolysis can be conveniently followed by the production of nitrophenolate ion which itself is measured by an increased absorption at 400 mµ. These esters appear to be hydrolysed at the same ‘active sites’ of the enzymes which are involved in the catalytic process with other synthetic or natural substrates3–6. Furthermore, when examining the effect of a given enzyme on a series of nitrophenyl esters with different substitutions in the acid portions, a pattern of specificity emerges which is fully comparable with that obtained with more conventional substrates5,7.

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Authors and Affiliations

  1. Department of Chemistry, Northwestern University, Evanston, and Abbott Laboratories, North Chicago

    L. LORAND & M. M. MOZEN

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  1. L. LORAND
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  2. M. M. MOZEN
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LORAND, L., MOZEN, M. Ester-hydrolysing Activity of Urokinase Preparations. Nature 201, 392–393 (1964). https://doi.org/10.1038/201392a0

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