1984
DOI: 10.1177/00220345840630081201
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Properties of Kininase in Rat Dental Pulp

Abstract: A kininase, capable of degrading bradykinin, was partially purified from the dental pulp of rats, and its properties were investigated. Chromatography on both Sephadex G-200 and DEAE Sephadex A-50 columns gave a single peak of kininase activity. The molecular weight of the enzyme, estimated by gel filtration, was about 67,000, and the optimum pH for the enzymatic reaction was about 7.5. The enzyme appears to contain a labile SH group(s) that is essential for its activity, because CdCl2, HgCl2 (0.1 mM each), an… Show more

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