Simultaneous purification and characterization of cytochrome b5 reductase and cytochrome b5 from sheep liver

Date

1999-02-01

Author

Arinc, E
Cakir, D

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Cytochrome b5 was purified from detergent solubilized sheep liver microsomes by using three successive DEAE-cellulose, and Sephadex G-100 column chromatographies. It was purified 54-fold and the yield was 23.5% with respect to microsomes. The apparent Mr of cytochrome b5 was estimated to be 16,200 +/- 500 by SDS-PAGE. Absolute absorption spectrum of the purified cytochrome b5 showed maximal absorption at 412 nm and dithionite-reduced cytochrome b5 gave peaks at 557, 526.5 and 423 nm. The ability of the purified sheep liver cytochrome b5 to transfer electrons from

Subject Keywords

Cell Biology, Biochemistry

URI

https://hdl.handle.net/11511/66098

Journal

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

DOI

https://doi.org/10.1016/s1357-2725(98)00099-5

Collections

Department of Biology, Article

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Citation Formats

E. Arinc and D. Cakir, “Simultaneous purification and characterization of cytochrome b5 reductase and cytochrome b5 from sheep liver,” INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, pp. 345–362, 1999, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/66098.