Metalloproteases of Serratia liquefaciens: degradation of purified human serum proteins.
Two representative strains of Serratia liquefaciens, SL 5 (serotype O5:H1) and SL 11 (serotype O1:H1), produced proteases characterized by molecular weights of 52.5 kilodaltons and isoelectric points of 6.2; both enzymes were inhibited by 50 mM EDTA. As demonstrated with SDS-PAGE electrophoresis, the two metalloproteases attacked the following purified human serum proteins: complement components C3, C4, C5, C6, C7, C8, and C9, transferrin, alpha 1-antitrypsin, alpha 2-macroglobulin, fibronectin, type III fibrinogen, immunoglobulin G (heavy chains), and IgM (heavy chains). However, C1q, IgA, haptoglobin, and C-reactive protein were refractory.
Wolf
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Institut für Medizinische Mikrobiologie und Hygiene, Universität des Saarlandes, Homburg/Saar.
Bauer
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Traub
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WH
D001798:Blood Proteins / Q000378:metabolism*; D003165:Complement System Proteins / Q000378:metabolism; D003429:Cross Reactions; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism; D007526:Isoelectric Point; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D012705:Serratia / Q000201:enzymology*; D014168:Transferrin / Q000378:metabolism; D000515:alpha 1-Antitrypsin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000378:metabolism
D001798:Blood Proteins; D005353:Fibronectins; D007136:Immunoglobulins; D011480:Protease Inhibitors; D014168:Transferrin; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins; D005340:Fibrinogen; D003165:Complement System Proteins; D004492:Edetic Acid; D008666:Metalloendopeptidases