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

Date

1991-01-01

Author

Güray, Nülüfer Tülün

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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.

Subject Keywords

Biochemistry

URI

https://hdl.handle.net/11511/48582

Journal

INTERNATIONAL JOURNAL OF BIOCHEMISTRY

DOI

https://doi.org/10.1016/0020-711x(91)90233-d

Collections

Department of Biology, Article

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Citation Formats

N. T. Güray, “KINETIC-PROPERTIES OF PURIFIED SHEEP LUNG MICROSOMAL NADH-CYTOCHROME B5 REDUCTASE,” INTERNATIONAL JOURNAL OF BIOCHEMISTRY, pp. 1315–1320, 1991, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/48582.