Abstract
ALTHOUGH the action of renin on the blood pressure has been explored by many investigators, some of its basic enzymatic properties are yet to be established1. While studying plasma kinins, we found it to be of advantage to couple enzymes that release or inactivate kinins covalently to water-insoluble complexes2–4. The active insoluble derivatives of enzymes are convenient to use, because, among many other attractive properties, they are stable, re-usable and readily removed from incubation mixture by sedimentation. We have extended these investigations to renin. Our previous results with killikrein, carboxypeptidases, kallikrein and trypsin inhibitors and renin were briefly reported3,4. This report deals with the binding of renin to ‘Sepharose 4B’.
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SEKI, T., JENSSEN, T., LEVIN, Y. et al. Active Water-insoluble Derivative of Renin. Nature 225, 864–865 (1970). https://doi.org/10.1038/225864a0
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DOI: https://doi.org/10.1038/225864a0
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