Abstract
Abstract A four-step procedure was utilized in the isolation of two complement-derived anaphylatoxins (C3a and C5a) from yeast cell activated human serum. Advantage was taken of one gel filtration and three ion exchange chromatographic steps to obtain two homogeneous products. The carboxypeptidase inhibitor epsilon-aminocaproic acid (EACA) was added to the serum to prevent inactivation of the anaphylatoxins during their generation. Purified C3a and C5a were judged to be homogeneous by sodium dodecyl sulfate polyacrylamide gel electrophoresis (PAGE), acid PAGE, and cellulose acetate strip electrophoresis. A single precipitin are was detected when each agent was challenged with the corresponding rabbit antibody after immunoelectrophoresis. Recovery of the respective anaphylatoxins from 1 liter of activated serum was 6 to 8 mg for C3a and 400 to 600 µg for C5a. A partial chemical characterization of the C5a revealed that arginine was released from the COOH-terminus by carboxypeptidase B digestion.
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