Abstract
NADH-cytochrome b5 reductase was isolated and partially purified from rabbit liver microsomes. It was immobilized into gelatin by chemical cross-linking. Chromium (III) acetate was used as cross-linker. The effects of pH and temperature on the immobilized cytochrome b5 reductase were investigated. The reusability and storage stability of immobilized enzyme were also tested. Immobilized NADH-cytochrome b5 reductase activities were found to be stable for at least 72 d and 24 uses. The storage stability of NADH-cytochrome b5 reductase was improved with immobilization at 25°C.
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