Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET

User menu

  • My alerts
  • Log in
  • My Cart

Search

  • Advanced search
Molecular Pharmacology
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET
  • My alerts
  • Log in
  • My Cart
Molecular Pharmacology

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Visit molpharm on Facebook
  • Follow molpharm on Twitter
  • Follow molpharm on LinkedIn
Research ArticleArticle

Accessibility of Cytochrome P450 in Microsomal Membranes: Inhibition of Metabolism by Antibodies to Cytochrome P450

PAUL E. THOMAS, ANTHONY Y. H. LU, SUSAN B. WEST, DENE RYAN, GERALD T. MIWA and WAYNE LEVIN
Molecular Pharmacology September 1977, 13 (5) 819-831;
PAUL E. THOMAS
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
ANTHONY Y. H. LU
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
SUSAN B. WEST
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
DENE RYAN
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
GERALD T. MIWA
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
WAYNE LEVIN
Department of Biochemistry and Drug Metabolism, Research Division, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & Metrics
  • eLetters
  • PDF
Loading

Abstract

Specific antibodies against highly purified cytochrome P450 from phenobarbital (PB)-treated rats and cytochrome P448 from 3-methycholanthrene (MC)-treated rats were produced in rabbits. These antibodies are inhibitors of drug metabolism catalyzed by liver microsomes from untreated rats or from rats treated with PB, MC, or pregnenolone-16α-carbonitrile (PCN). Microsomal metabolism of five substrates was examined; the extent of antibody inhibition was dependent not only on the source of the antibody and microsomes but also on the specific substrate and the reactions catalyzed. A comparison of the antibody inhibition patterns of the various substrates examined indicates a marked difference in the proportions of the different forms of cytochrome P450 present in liver microsomes from untreated and PB-, MC-, and PCN-treated rats. Antibody inhibition of microsomal metabolism indicates that the membrane-bound terminal oxidase, cytochrome P450 or P448, is at least partially exposed to the hydrophilic environment on the exterior of microsomal membranes.

ACKNOWLEDGMENTS We thank Ms. Candy Caso and Ms. Carla Cable for help in preparing the manuscript.

  • Copyright © 1977 by Academic Press, Inc.

MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years. 

Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page. 

 

  • Click here for information on institutional subscriptions.
  • Click here for information on individual ASPET membership.

 

Log in using your username and password

Forgot your user name or password?

Purchase access

You may purchase access to this article. This will require you to create an account if you don't already have one.
PreviousNext
Back to top

In this issue

Molecular Pharmacology
Vol. 13, Issue 5
1 Sep 1977
  • Table of Contents
  • Table of Contents (PDF)
  • Index by author
  • Back Matter (PDF)
  • Editorial Board (PDF)
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for sharing this Molecular Pharmacology article.

NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.

Enter multiple addresses on separate lines or separate them with commas.
Accessibility of Cytochrome P450 in Microsomal Membranes: Inhibition of Metabolism by Antibodies to Cytochrome P450
(Your Name) has forwarded a page to you from Molecular Pharmacology
(Your Name) thought you would be interested in this article in Molecular Pharmacology.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
Research ArticleArticle

Accessibility of Cytochrome P450 in Microsomal Membranes: Inhibition of Metabolism by Antibodies to Cytochrome P450

PAUL E. THOMAS, ANTHONY Y. H. LU, SUSAN B. WEST, DENE RYAN, GERALD T. MIWA and WAYNE LEVIN
Molecular Pharmacology September 1, 1977, 13 (5) 819-831;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero

Share
Research ArticleArticle

Accessibility of Cytochrome P450 in Microsomal Membranes: Inhibition of Metabolism by Antibodies to Cytochrome P450

PAUL E. THOMAS, ANTHONY Y. H. LU, SUSAN B. WEST, DENE RYAN, GERALD T. MIWA and WAYNE LEVIN
Molecular Pharmacology September 1, 1977, 13 (5) 819-831;
Reddit logo Twitter logo Facebook logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Jump to section

  • Article
  • Info & Metrics
  • eLetters
  • PDF

Related Articles

Cited By...

More in this TOC Section

  • Antimicrobial and Antileukemic Transportan 10 Conjugates
  • Pharmacological characterization of zebrafish H1 receptor
  • Bhave and Forman
Show more Article

Similar Articles

Advertisement
  • Home
  • Alerts
Facebook   Twitter   LinkedIn   RSS

Navigate

  • Current Issue
  • Fast Forward by date
  • Fast Forward by section
  • Latest Articles
  • Archive
  • Search for Articles
  • Feedback
  • ASPET

More Information

  • About Molecular Pharmacology
  • Editorial Board
  • Instructions to Authors
  • Submit a Manuscript
  • Customized Alerts
  • RSS Feeds
  • Subscriptions
  • Permissions
  • Terms & Conditions of Use

ASPET's Other Journals

  • Drug Metabolism and Disposition
  • Journal of Pharmacology and Experimental Therapeutics
  • Pharmacological Reviews
  • Pharmacology Research & Perspectives
ISSN 1521-0111 (Online)

Copyright © 2023 by the American Society for Pharmacology and Experimental Therapeutics