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


Arinc E., Cakir D.

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, vol.31, no.2, pp.345-362, 1999 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 2
  • Publication Date: 1999
  • Doi Number: 10.1016/s1357-2725(98)00099-5
  • Title of Journal : INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
  • Page Numbers: pp.345-362

Abstract

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