A 41.7 kDa serine protease from Clostridium perfringens type A: degradation of purified human serum proteins.
Two clinical isolates of Clostridium perfringens type A produced a novel caseinolytic serine protease. Both enzymes had a molecular weight of 41.7 kilodaltons and an isoelectric point of 9.1. The two enzymes were immunogenic for rabbits and closely related serologically. Both enzymes partially degraded the heavy chains of human immunoglobulins (Ig) G and IgM, but not IgA. Purified human complement (C) components C3, C5, C8, and C9 were attacked; C1q was refractory. Both enzymes were active against human transferrin, alpha 1-antitrypsin, alpha 2-macroglobulin, haptoglobin, type III fibrinogen, and fibronectin. C-reactive protein was refractory.
Wolf
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U
Institut für Medizinische Mikrobiologie und Hygiene, Universität des Saarlandes, Homburg/Saar, Germany.
Bauer
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Traub
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WH
D001798:Blood Proteins / Q000378:metabolism*; D015153:Blotting, Western; D002851:Chromatography, High Pressure Liquid; D003016:Clostridium perfringens / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D012697:Serine Endopeptidases / Q000378:metabolism*
D001798:Blood Proteins; D012697:Serine Endopeptidases