Characterization and purification of biliverdin reductase from the liver of eel,Anguilla japonica |
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| Affiliation: | 1. Research Unit in Environmental and Evolutionary Biology, Université de Namur, rue de Bruxelles 61, B-5000, Namur, Belgium;2. The Smoler Proteomics Center, Emerson Life Science Building, Technion–Israel Institute of Technology, 32000 Haifa, Israel;1. INRA, UMR 1224 Ecobiop, Aquapôle, 64310 Saint Pée sur Nivelle, France;2. Université de Pau et des Pays de L''Adour, UMR 1224 Ecobiop, UFR Sciences et Techniques côte Basque, Anglet, France;3. Univ. Bordeaux, UMR CNRS 5805 EPOC, Team Aquatic Ecotoxicology, Place du Dr Peyneau, 33120 Arcachon, France;4. Laboratoire de Chimie Analytique Bio-Inorganique et Environnement, Institut Pluridisciplinaire de Recherche sur l''Environnement et les Matériaux, UMR 5254 CNRS, Université de Pau et des Pays de l''Adour, A Pau, France;1. Département de biologie, Université de Moncton, Moncton, NB E1A 3E9, Canada;2. Laboratoire de Biologie Intégrative et Évolutive, Université du Québec à Rimouski, Rimouski, Québec G5L 3A1, Canada;3. Division des Collections Vivantes et de la Recherche, Biodôme de Montréal-Espace pour la vie, Montréal, Québec H1X 2B2, Canada;4. Département de chimie et biochimie, Université de Moncton, Moncton, NB E1A 3E9, Canada |
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| Abstract: | - 1.1. Biliverdin reductase from the liver of eel, Anguilla japonica was characterized and purified with a novel enzymatic staining method on polyacrylamide electrophoretic gel.
- 2.2. This enzyme could use both NADPH and NADH as coenzyme. The Km of NADPH was 5.2 μM, while that of NADH was 5.50 μM.
- 3.3. The optimum reaction pH for using HADPH as coenzyme was 5.3. That for NADH was 6.1. The optimum reaction temperature is 37°C.
- 4.4. When NADPH was used as coenzyme, the Km of biliverdin was 0.6 μM. When NADH was used as coenzyme, the Km of biliverdin was 7.0 μM.
- 5.5. The activity of the enzyme was inhibited by the concentration of biliverdin. Also, the potency of the enzyme was much less than that of the analogous enzyme isolated from mammals.
- 6.6. This is a fairly stable enzyme with a mol. wt around 67,000. Its estimated pI was pH 3.5–4.0.
- 7.7. This is the first time biliverdin reductase has been isolated and characterized from a vertebrate other than mammals. The property of it is quite different from that of mammals.
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