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

Date

1994-06-01

Author

Yıldırım, Onur
Akbulut, Ural
ARINC, E
SUNGUR, S

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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.

Subject Keywords

Biophysics, Mechanics of Materials, Bioengineering, Biomaterials, Ceramics and Composites

URI

https://hdl.handle.net/11511/36660

Journal

BIOMATERIALS

DOI

https://doi.org/10.1016/0142-9612(94)90208-9

Collections

Department of Economics, Article

Citation Formats

O. Yıldırım, U. Akbulut, E. ARINC, and S. SUNGUR, “STABILITY AND STORAGE-CONDITIONS OF NADH-CYTOCHROME B5 REDUCTASE CROSS-LINKED INTO GELATIN BY CHROMIUM(III) ACETATE,” BIOMATERIALS, vol. 15, no. 8, pp. 587–592, 1994, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/36660.