STABILITY AND STORAGE-CONDITIONS OF NADH-CYTOCHROME B5 REDUCTASE CROSS-LINKED INTO GELATIN BY CHROMIUM(III) ACETATE

YILDIRIM O., AKBULUT U., ARINC E., SUNGUR S.

BIOMATERIALS, vol.15, no.8, pp.587-592, 1994 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 15 Issue: 8
  • Publication Date: 1994
  • Doi Number: 10.1016/0142-9612(94)90208-9
  • Journal Name: BIOMATERIALS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.587-592
  • Middle East Technical University Affiliated: Yes

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 degrees C.