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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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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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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
Citation Formats
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BibTeX
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
, vol. 31, no. 2, pp. 345–362, 1999, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/66098.