Kinetic Analysis of Lauric Acid Hydroxylation by Human Cytochrome P450 4A11-Reference-Cited by-同舟云学术

Kinetic Analysis of Lauric Acid Hydroxylation by Human Cytochrome P450 4A11

Published:2014-09-19 Issue:39 Volume:53 Page:6161-6172
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kim Donghak¹²,Cha Gun-Su³,Nagy Leslie D.¹,Yun Chul-Ho³,Guengerich F. Peter¹

Affiliation:

1. Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, United States

2. Department of Biological Sciences, Konkuk University, Seoul 143-701, Republic of Korea

3. School of Biological Sciences and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea

Funder

National Institute of Diabetes and Digestive and Kidney Diseases

National Cancer Institute

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi500710e

Reference78 articles.

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

2. Purified liver microsomal cytochrome P-450. Separation and characterization of multiple forms.

3. Human Cytochrome P450 Enzymes

4. cDNA cloning and inducible expression during pregnancy of the mRNA for rabbit pulmonary prostaglandin omega-hydroxylase (cytochrome P-450p-2).

5. Purification and Characterization of Two Forms of Fatty Acid ω-Hydroxylase Cytochrome P-450 from Rabbit Kidney Cortex Microsomes1

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