RESUMO
The enzymes (uricase (EC 1.7.3.3), allantoinase (EC 3.5.3.4), and allantoicase (EC 3.5.2.5) which participate in degradation of purine bases, were embedded separately in fibrin membranes formed by fibrinogen-fibrin conversion with thrombin. All of these enzymes together with catalase were also embedded in a single fibrin membrane to make an immobilized multienzyme complex. The multienzyme complex in fibrin membrane thus prepared had an ability of degradation of uric acid to urea and glyoxylic acid via allantoin and allantoic acid. The stability of immobilized uricase or catalase embedded in fibrin membrane upon lyophilization was also tested in a comparison with nonimmobilized enzymes.
Assuntos
Amidoidrolases/metabolismo , Catalase/metabolismo , Enzimas Imobilizadas/metabolismo , Fibrina , Complexos Multienzimáticos/metabolismo , Urato Oxidase/metabolismo , Ureo-Hidrolases/metabolismo , Acetatos , Alantoína , Animais , Candida/enzimologia , Bovinos , Fibrinogênio , Cinética , Fígado/enzimologia , Saccharomyces cerevisiae/enzimologia , Ureia/análogos & derivadosRESUMO
Transglutaminase from guinea pig liver catalyzed the formation of cross-links between fibrinogen (or fibrin) and ribonuclease. Using transglutaminase, immoblized ribonuclease was prepared by two separate methods: (1) fibrinogen-ribonuclease conjugates formed by transglutaminase were treated with thrombin to make fibrin membrane bound covalently to the enzyme; (2) fibrin polymer formed from fibrinogen with thrombin was covalently bound to ribonuclease by transglutaminase to make fibrin-ribonuclease conjugates.