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Biliverdin reductase was characterized and purified from the liver of Atlantic salmon (Salmo salar) using a novel enzymatic staining method. The properties of the enzyme are quite different from those of mammals. The purified enzyme is a monomeric protein with a molecular weight of approximately 68 kD and an isoelectric point of around 3.8. The enzyme can utilize both NADH and NADPH as coenzyme, but...
Biliverdin IXα was purified from the bile of Atlantic salmon (Salmo salar) using a silica gel (Wakogel C-200) column. The yield was 49.5 mg per 100 ml of fresh bile and purity 95.3%. The biliverdin IXα in the bile was quite stable when the bile was frozen at –80°C for a period of 40 days. However, 7.1% of the biliverdin IXα was lost when the bile was stored at 4°C for 20 days. The purified biliverdin...
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