The complement-derived peptides C5a and C5adesArg (highly purified from yeast-activated hog serum) were both active in the following biological assays: in aggregation of human leukocytes (potency ratio for C5a:C5adesArg 3:1), in aggregation of guinea pig platelets (10:1), in chemotaxis of peritoneal rabbit leukocytes (10:1), and in contraction of isolated guinea pig ileum (2.4:1). The fact that C5adesArg preparations have 30 and 40% of the activity of C5a in leukocyte aggregation and smooth muscle contraction but only 10% of C5a chemotactic activity, clearly indicates that aggregation and spasmogenic activity are inherent properties of C5adesArg. Evidence that C5adesArg owns all activities studied is further given by the following findings: chromatographic separation of mixtures of C5a and C5adesArg results in the appearance of two peaks of spasmogenic activity; treatment of C5adesArg with carbopeptidase B does neither lead to release of detectable arginine nor abrogate any of the biological effects; treatment of C5a with carboxypeptidase B reduces the activities quantitatively to those of C5adesArg, and liberates the theoretically expected amount of arginine.

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© 1980 S. Karger AG, Basel
1980
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