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Structure and Function of Invertebrate Oxygen Carriers

  • Conference proceedings
  • © 1991

Overview

Editors:
  1. Serge N. Vinogradov

    1. Biochemistry Department, Wayne State University School of Medicine, Detroit, USA

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  2. Oscar H. Kapp

    1. Enrico Fermi Institute, University of Chicago, Chicago, USA

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Table of contents (45 papers)

  1. Front Matter

    Pages i-xxiv
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  2. Quarternary and Three-Dimensional Structure

    1. Front Matter

      Pages xxv-xxv
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    2. The Architecture of 4x6-meric Arachnid Hemocyanin

      • Nicolas Boisset, Jean-Christophe Taveau, Jean Lamy
      Pages 1-8

    3. Static and Kinetic Studies on the Dissociation of Limulus polyphemus Hemocyanin with Solution X-Ray Scattering

      • Kazumoto Kimura, Yoshihiko Igarashi, Akihiko Kajita, Zhi-Xin Wang, Hirotsugu Tsuruta, Yoshiyuki Amemiya et al.
      Pages 9-18

    4. The Di-decameric Hemocyanin of the Atlantic Murex Snail, Muricanthus fulvescens (Sowerby)

      • Theodore T. Herskovits, Curley Kieran, Michelle D. Edwards, Mary G. Hamilton
      Pages 19-24

    5. Scanning Transmission Electron Microscopy (STEM) Studies of Molluscan Hemocyanins

      • Mary G. Hamilton, Theodore T. Herskovits, Joseph S. Wall
      Pages 25-32

    6. Spectroscopic Analysis of Temperature-Induced Unfolding of the Hemocyanin from the Tarantula Eurypelma californicum

      • Franz Penz, Heinz Decker
      Pages 33-36

    7. Subunit Structure of the Hemocyanin from the Arthropod Ovalipes catharus

      • H. David Ellerton, Nik Rahimah Husain
      Pages 37-48

    8. Crosslinking with Bifunctional Reagents and its Application to the Determination of the Quaternary Structures of Invertebrate Extracellular Hemoglobins

      • Abdussalam Azem, Amnon Pinhasy, Ezra Daniel
      Pages 49-57

    9. Arthropod (Cyamus scammoni, Amphipoda) Hemoglobin Structure and Function

      • Nora B. Terwilliger
      Pages 59-63

    10. The Principal Subunit of Earthworm Hemoglobin is a Dodecamer of Heme-Containing Chains

      • Pawan K. Sharma, Aziz N. Qabar, Oscar H. Kapp, Joseph S. Wall, Serge N. Vinogradov
      Pages 65-72

    11. Heterogeneity of the Products of Dissociation of Lumbricus terrestris Hemoglobin at Alkaline pH

      • Pawan K. Sharma, Serge N. Vinogradov, Daniel A. Walz
      Pages 73-77

    12. Studies on the Dissociation of Eudistylia vancouverii Chlorocruorin

      • Aziz N. Qabar, Oscar H. Kapp, Joseph S. Wall, Serge N. Vinogradov
      Pages 79-86

  3. Structure and Function

    1. Front Matter

      Pages 87-87
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    2. Nested Allostery of Arthropod Hemocyanins

      • Heinz Decker
      Pages 89-98

    3. Subunits and Cooperativity of Procambarus clarki Hemocyanin

      • Nobuo Makino, Hiromi Ohnaka
      Pages 99-107

    4. Analysis of Oxygen Equilibrium Using the Adair Model for the Hemocyanin of Limulus polyphemus and the Hemoglobin of Eisenia foetida

      • Yoshihiko Igarashi, Kazumoto Kimura, Zhi-Xin Wang, Akihiko Kajita
      Pages 109-113

    5. Structural and Functional Characterization of the Hemoglobin from Lumbricus terrestris

      • Kenzo Fushitani, Austen F. Riggs
      Pages 115-120

    6. Interaction of Divalent Metal Ions with the Hemoglobin of Glossoscolex paulistus: an EPR Study

      • Marcel Tabak, Maria H. Tinto, Hidetake Imasato, Janice R. Perussi
      Pages 121-125

    7. Oxidation of the Extracellular Hemoglobin of Glossoscolex paulistus

      • Janice R. Perussi, Adalto R. de Souza, Maria H. Tinto, Hidetake Imasato, Nilce C. Meirelles, Marcel Tabak
      Pages 127-131
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Keywords

About this book

Oxygen binding proteins are large multi unit proteins ideally suited for the study of structure function relationships in biological molecules. This book, based on a Symposium at the Xth International Biophysics Congress in 1990, provides a synthesis of recent advances in our knowledge of invertebrate oxygen carriers such as hemoglobins, hemocyanins, and hemorythrins. Comprehensive reviews are combined with new research results of importance to all biochemists and molecular biologists interested in oxygen carriers in general, their gene structure and comparative biochemistry. Of particular value are the studies of invertebrate oxygen binding proteins which perform their function and have structures vastly different from the vertebrate hemoglobins and myoglobins, as well as numerous examples of modern molecular techniques as applied to research on this diverse group of proteins.

Editors and Affiliations

  • Biochemistry Department, Wayne State University School of Medicine, Detroit, USA

    Serge N. Vinogradov

  • Enrico Fermi Institute, University of Chicago, Chicago, USA

    Oscar H. Kapp

Bibliographic Information

  • Book Title: Structure and Function of Invertebrate Oxygen Carriers

  • Editors: Serge N. Vinogradov, Oscar H. Kapp

  • DOI: https://doi.org/10.1007/978-1-4612-3174-5

  • Publisher: Springer New York, NY

  • eBook Packages: Springer Book Archive

  • Copyright Information: Springer-Verlag New York, Inc. 1991

  • Softcover ISBN: 978-1-4612-7825-2Published: 08 October 2011

  • eBook ISBN: 978-1-4612-3174-5Published: 06 December 2012

  • Edition Number: 1

  • Number of Pages: XXV, 352

  • Topics: Zoology

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