Stability and storage conditions of NADH-cytochrome b5 reductase cross-linked into gelatin by chromium (III) acetate.
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 degrees C.
Yildirim
O
O
Department of Biology, Ankara University, Sciences Faculty, Turkey.
Akbulut
U
U
Arinç
E
E
Sungur
S
S
D000085:Acetates; D019342:Acetic Acid; D000818:Animals; D003432:Cross-Linking Reagents; D003579:Cytochrome Reductases / Q000737:chemistry* / Q000302:isolation & purification; D042966:Cytochrome-B(5) Reductase; D004356:Drug Storage; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005780:Gelatin; D006863:Hydrogen-Ion Concentration; D008862:Microsomes, Liver; D011817:Rabbits; D013696:Temperature
D000085:Acetates; D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D005780:Gelatin; D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase; D019342:Acetic Acid