Water-Soluble Macromolecular Complexes of Kallikrein, Bradykinin and Inhibitors of Kallikrein and Kininase II.
TEXAS UNIV HEALTH SCIENCE CENTER AT DALLAS
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Pig pancreatic kallikrein, aprotinin Trasylol, SQ 21541, an angiotensin I converting enzyme or kininase II inhibitor, and bradykinin were each coupled covalently to soluble dextran m.w. 500,000. Dextran had been activated either with cyanogen bromide or sodium meta-periodate. Of the reactants, 23 to 56 were bound to activated dextrans. The activities of the complexes were determined in vitro by spectrophotometric technique or radioimmunoassay and bioassay. Depending on the mode of coupling and the test employed soluble macromolecular complexes retained 6 to 92 of the in vitro activity of the native compound. Bradykinin coupled covalently to dextran was inactivated slower by converting enzyme than was free bradykinin. Author