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Cited by 627

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

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

Open access
Lu, A Y H, Coon, M J·1968·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)56992-7
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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.

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Metadata

Authors
Lu, A. Y. H., & Coon, M. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1968-03
Volume
243
Issue
6
Pages
1331-1332
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)56992-7
OpenAlex
W1673905022
Cited by
627
References
1
FWCI
33.41
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes. https://app.cochat.ai/papers/10.1016/s0021-9258(19)56992-7
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Lu, A. Y. H., & Coon, M. J. (1968). Role of Hemoprotein P-450 in Fatty Acid ω-Hydroxylation in a Soluble Enzyme System from Liver Microsomes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)56992-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.