Abstracts of Papers Presented at the Third International Complement Workshop, Harvard Medical School, Boston, Massachusetts, June 3–5, 1968

[摘要] The development of a hemolytic assay for the measurement of the inhibitor of the first component of complement (C′1aINH) and the isolation of physically homogeneous and functionally pure human plasma kallikrein have permitted studies evaluating the possible interrelation of the complement and kinin-forming systems. It was demonstrated that C′1aINH inhibited the action of kallikrein on the synthetic substrate, p -toluene sulfonyl l-arginine methyl ester (TAMe). It was further observed that consumption of C′laINH exhibited a concentration and time dependence similar to its interaction with C′1 esterase. Kinetic analysis suggested the formation of an inactive stoichiometric complex of kallikrein and C′1aINH. Similar observations were made utilizing a highly purified preparation of C′1aINH supplied by Dr. J. Pensky. In contrast, C′laINH failed to inhibit plasmin, trypsin, and thrombin; and inactivation of C′1aINH by plasmin did not occur except at very high enzyme concentrations. Sera from patients lacking C′laINH failed to inhibit the TAMe esterase activity of plasma kallikrein, while sera deficient in α1-antitrypsin but containing normal amounts of C′1aINH were equally inhibitory as normal sera.

[学科分类] 生物科学（综合）