TRYPSIN-ACTIVATED COMPLEX OF HUMAN FACTOR-B WITH COBRA VENOM FACTOR (CVF), CLEAVING C3 AND C5 AND GENERATING A LYTIC FACTOR FOR UNSENSITIZED GUINEA-PIG ERYTHROCYTES .1. GENERATION OF ACTIVATED COMPLEX

  • 1 January 1975
    • journal article
    • research article
    • Vol. 18  (4) , 193-204
Abstract
A complex formed between CVF and isolated human factor B [the 3rd component of complement (C3) proactivator] (B) was converted by trypsin to a stable enzyme, CVF-.hivin.B which cleaved C3 and C5 of human C. The formation of CVF-.hivin.B by trypsin required divalent cations; the formation of the lytic factor from human serum occurred even in the presence of EDTA. CVF-.hivin.B purifed by gel filtration could initiate the hemolysis of unsensitized guinea pig erythrocytes when incubated with human C components C5-C9 in 0.01 M EDTA buffer. C3 was not required for the lysis of guinea pig erythrocytes initiated by CVF-.hivin.B, because the .beta.1C [globulin with C3 activity] precipitation line formed between human serum and [rabbit] anti-.beta.1C antibody did not inhibit the hemolysis by CVF-.hivin.B in agarose gel. Treatment of .beta.1C and .beta.1F [globulin with C5 activity] in whole human serum with CVF-.hivin.B in the presence of 0.01 M EDTA converted them to components with higher mobilities on immunoelectrophoresis.

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