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Cytochromes P-450 and b5

Structure, Function, and Interaction

  • Book
  • © 1975

Overview

Editors:
  1. David Y. Cooper

    1. Harrison Department of Surgical Research, University of Pennsylvania School of Medicine, Philadelphia, USA

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  2. Otto Rosenthal

    1. Harrison Department of Surgical Research, University of Pennsylvania School of Medicine, Philadelphia, USA

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  3. Robert Snyder

    1. Department of Pharmacology, Thomas Jefferson University, Philadelphia, USA

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  4. Charlotte Witmer

    1. Department of Pharmacology, Thomas Jefferson University, Philadelphia, USA

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Part of the book series: Advances in Experimental Medicine and Biology (AEMB, volume 58)

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Table of contents (34 chapters)

  1. Front Matter

    Pages i-xiii
    Download chapter PDF

  2. Session I

    1. Part 1

      1. Partial Purification and Separation of Multiple Forms of Cytochrome P-450 and Cytochrome P-448 from Rat Liver Microsomes
        • W. Levin, A. Y. H. Lu, D. Ryan, S. West, R. Kuntzman, A. H. Conney
        Pages 1-24
      2. Biochemical Characterization of Highly Purified Cytochrome P-450 and Other Components of the Mixed Function Oxidase System of Liver Microsomal Membranes
        • Minor J. Coon, Theodore A. van der Hoeven, David A. Haugen, F. Peter Guengerich, Janice L. Vermilion, David P. Ballou
        Pages 25-46
      3. Immunochemical and Compositional Comparison of Cytochrome P-450<sub>cam</sub> of <u>Pseudomonas Putida</u> and P-450<sub>LM</sub> of Phenobarbital-Induced Rabbit Liver Microsomes
        • Karl Dus, William J. Litchfield, Anne G. Miguel, Theodore A. van der Hoeven, David A. Haugen, William L. Dean et al.
        Pages 47-53
      4. Immunochemical and Functional Similarities and Differences among Iron-Sulfur Proteins Involved in Mammalian Steroidogenesis
        • Jeffrey Baron
        Pages 55-71
      5. General Discussion
        • David Y. Cooper, Otto Rosenthal, Robert Snyder, Charlotte Witmer
        Pages 73-80

    2. Part 2

      1. Comparison of the Induction Course, Biophysical Chemical Interactions and Photochemical Action Spectra of Phenobarbital and 3-Methylcholanthrene Induced Hepatic Microsomal P-450
        • D. Y. Cooper, H. Schleyer, J. H. Thomas, H. M. Vars, O. Rosenthal
        Pages 81-102
      2. Cytochrome P-450 in the Activation and Inactivation of Carcinogens
        • Helmut Greim, Peter Czygan, Anthony J. Garro, Ferenc Hutterer, Fenton Schaffner, Hans Popper et al.
        Pages 103-115
      3. Effect of Cyclic Amp on the Phenobarbital Induced Increase in Cytochrome P-450 and Hypertrophy of the Endoplasmic Reticulum of the Rat Liver
        • Ferenc Hutterer, Kenneth Dressler, Helmut Greim, Peter Czygan, Fenton Schaffner, Hans Popper
        Pages 117-126
      4. Evidence for the Activation of 3-Methylcholanthrene as a Carcinogen <u>in vivo</u> and as a Mutagen <u>in vitro</u> by P<sub>1</sub>-450 from Inbred Strains of Mice
        • Daniel W. Nebert, James S. Felton
        Pages 127-149
      5. Increased Translation as a Result of Elevated Initiation Factor Activity after Administration of 3-Methylcholanthrene
        • Edward Bresnick, John Hopkinson, P. M. Prichard
        Pages 151-164
      6. Discussion
        • David Y. Cooper, Otto Rosenthal, Robert Snyder, Charlotte Witmer
        Pages 165-173

  3. Session II

    1. Part 1

      1. Optical and Electron Paramagnetic Resonance Studies of Partially Purified Rabbit Liver Cytochrome P-450
        • Charlotte Witme, Peter Nehls, Peter Krauss, Herbert Remmer, Robert Snyder
        Pages 175-187
      2. Studies on the Spin State of 3-Methylcholanthrene Induced Cytochrome P-450 from Rat Liver
        • J. O. Stern, E. Peisach, J. Peisach, W. E. Blumberg, A. Y. H. Lu, S. West et al.
        Pages 189-202
      3. An Analysis of the Optical Titrations of the 430 and 455 NM Chromophores of Ethyl Isocyanide Complexes of Mammalian Hepatic Cytochrome P-450
        • J. Peisach
        Pages 203-212
      4. Implication of Ligand Modified Spectra of Cytochrome P-450 Associated with Pregnenolone Synthesis in Mitochondria from Corpus Luteum
        • V. I. Uzgiris, E. N. McIntosh, P. Graves, H. A. Salhanick
        Pages 213-227
      5. General Discussion
        • David Y. Cooper, Otto Rosenthal, Robert Snyder, Charlotte Witmer
        Pages 229-237

    2. Part 2

      1. Studies on the Interaction of Water with Microsomal Cytochrome P-450
        • Jordan L. Holtzman
        Pages 239-249
      2. Drug Metabolism in Isolated Rat Liver Cells
        • Robert Grundin, Peter Moldéus, Helena Vadi, Sten Orrenius, Christer von Bahr, Dan Bäckström et al.
        Pages 251-269
      3. Role of Phospholipids in Adrenocortical Microsomal Hydroxylation Reactions: Activation of Lipid-Depleted Microsomal Preparations by Non-Ionic Detergents
        • Shakunthala Narasimhulu
        Pages 271-286
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Keywords

About this book

P-450 has in common with our nation that it can call Phila­ delphia its hometown. Yet there are differences, too. The U. S. A. was born and named in this city. P-450 was first recog­ nized here -- an odd CO-combining pigment without family or func­ tion. Japanese workers identified it as an unusual member of the cytochrome family. Finally, in Philadelphia, its biological func­ tion was established and its growth to a global power initiated. Since discovery of its function as terminal oxidase of the 21-steroid hydroxylase system of adrenocortical microsomes, P-450 has proved to play the same role in a wide variety of other mixed function oxidase systems involved in biosynthesis and catabolism of specific cell or body components as well as in the metabolism of foreign substances entering organisms. P-450-like oxygenating enzymes appear to be fundamental cellular constituents in most forms of aerobic organisms. Activation of molecular oxygen and incorporation of one of its atoms into organic compounds as cata­ lyzed by P-450 enzymes are reactions of vital importance not only for biosynthesis and degradation of steroid hormones necessary for sustaining life, but also for metabolic activation or inactivation of foreign agents such as drugs, food preservatives and additives, insecticides and carcinogens. Moreover, P-450 linked enzyme sys­ tems can either be induced or suppressed by these agents with significant biological consequences.

Editors and Affiliations

  • Harrison Department of Surgical Research, University of Pennsylvania School of Medicine, Philadelphia, USA

    David Y. Cooper, Otto Rosenthal

  • Department of Pharmacology, Thomas Jefferson University, Philadelphia, USA

    Robert Snyder, Charlotte Witmer

Bibliographic Information

  • Book Title: Cytochromes P-450 and b5

  • Book Subtitle: Structure, Function, and Interaction

  • Editors: David Y. Cooper, Otto Rosenthal, Robert Snyder, Charlotte Witmer

  • Series Title: Advances in Experimental Medicine and Biology

  • DOI: https://doi.org/10.1007/978-1-4615-9026-2

  • Publisher: Springer New York, NY

  • eBook Packages: Springer Book Archive

  • Copyright Information: The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 1975

  • Softcover ISBN: 978-1-4615-9028-6Published: 12 December 2012

  • eBook ISBN: 978-1-4615-9026-2Published: 06 December 2012

  • Series ISSN: 0065-2598

  • Series E-ISSN: 2214-8019

  • Edition Number: 1

  • Number of Pages: XIII, 554

  • Topics: Animal Anatomy / Morphology / Histology

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