ISOLATION AND CHARACTERIZATION OF FIBRINOGENASE FROM CANDIDA-ALBICANSNH-1

1. Fibrinogenase was isolated from Candida albicans NH-I by DEAE-Cellu lose, Sephadex G-75 and Sephadex G-100 column chromatographies. 2. The purified fibrinogenase gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate polya crylamide gel electrophoresis. 3. The enzyme preparation had a molecul ar weight of 13,000, isoelectric point of pH 4.2 and possessed 117 ami no acid residues. 4. The purified fibrinogenase possessed capillary pe rmeability-increasing activity. 5. The enzyme hydrolyzed fibrinogen, c asein, hide powder azure, azocoll hydrolytic activities and also hydro lyzed the oxidized B chain of insulin. The cleavage sites in the oxidi zed B chain of insulin were identified as Asp(3)-Glu(4), Glu(13)-Ala(1 4), Ala(14)-Leu(17), Tyr(16)-Leu(17), Arg(22)-Gly(23), Phe(25)Tyr(26) and Tyr(26)-Thr(27). 6. Fibrinogenase activity of this preparation was inhibited by alpha(2)-macroglobulin antithrombin-III, omicron-phenant hroline, disodium ethylenediaminetetra acetic acid and dithiothreitol.