KINETIC-PROPERTIES OF PURIFIED SHEEP LUNG MICROSOMAL NADH-CYTOCHROME B5 REDUCTASE


GURAY T. , ARINC E.

INTERNATIONAL JOURNAL OF BIOCHEMISTRY, vol.23, no.11, pp.1315-1320, 1991 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 23 Issue: 11
  • Publication Date: 1991
  • Doi Number: 10.1016/0020-711x(91)90233-d
  • Title of Journal : INTERNATIONAL JOURNAL OF BIOCHEMISTRY
  • Page Numbers: pp.1315-1320

Abstract

1. Lung NADH-cytochrome b5 reductase was saturated with its artificial substrate, potassium ferricyanide at approximately 0.1 mM ferricyanide concentration, and the activity of the lung enzyme was inhibited by the higher concentrations of potassium ferricyanide. Ferricyanide at 0.5 and 1.0 mM inhibited the activity of the enzyme by about 20 and 61% respectively. The apparent K(m) value was calculated as 13.7-mu-M potassium ferricyanide and 4.3-mu-M NADH.