Work

Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes

Year: 1968

Type: article

Abstract: An enzyme system which catalyzes the ω-hydroxylation of fatty acids in the presence of reduced triphosphopyridine nucleotide and molecular oxygen has been obtained in a soluble form from rabbit liver microsomes. Three components have been separated from the microsomal extract and shown to be required for the conversion of laurate to ω-hydroxylaurate. These have been identified as hemoprotein P-450 (the carbon monoxide-binding pigment of microsomes), TPNH-cytochrome c reductase, and a heat-stable factor.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)56992-7

Authors: A Y H Lu, M J Coon

Institution: University of Michigan

Language: English

Topic: Pharmacogenetics and Drug Metabolism

Subfield: Pharmacology

Field: Pharmacology, Toxicology and Pharmaceutics

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1673905022

FWCI: 21.27

Cites: 19

Cited by: 623

Related to: 9