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Biochemical and Clinical Aspects of Hemoglobin Abnormalities - 1st Edition - ISBN: 9780121643508, 9780323142748

Biochemical and Clinical Aspects of Hemoglobin Abnormalities

1st Edition

Editor: Winslow Caughey
Paperback ISBN: 9780124123595
eBook ISBN: 9780323142748
Hardcover ISBN: 9780121643508
Imprint: Academic Press
Published Date: 1st January 1978
Page Count: 746
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Biochemical and Clinical Aspects of Hemoglobin Abnormalities contains the proceedings of a symposium held on the Pingree Park campus of Colorado State University on October 2-7, 1977. Contributors discuss the biochemical and clinical aspects of hemoglobin abnormalities and cover topics ranging from amino acid substitutions to sickle cell disease, glycosylated hemoglobins, cystamine inhibition of sickling, and gelation of sickle cell hemoglobin. This volume is organized into 52 chapters and begins with a discussion of the role of distal residues in structure, ligand binding, and oxidation of hemoglobins A, Zurich, and Sydney. It then turns to functional abnormalities of whole blood in sickle cell anemia, inhibition of sickle hemoglobin gelation by amino acids and peptides, and intermolecular interactions in crystals of human deoxy hemoglobins A, C, F, and S. The chapters that follow focus on glycosylation of human hemoglobin, the phase transitions of sickle-cell hemoglobin, conformational effects of the HbS mutation, and mechanisms for hemoglobin oxidation. The reader is also introduced to oxidation of oxyhemoglobin by reductants, the kinetics of oxygen binding to human red blood cells, and oxidation of human hemoglobin by copper. A chapter that assesses the effect of physiological parameters, such as pH, oxygen concentration, protein concentration, non-gelling hemoglobins, and the erythrocyte membrane, on the kinetics of polymerization of deoxyhemoglobin S concludes the book. This book is intended for biochemists and clinicians interested in knowing more about hemoglobin abnormalities.

Table of Contents

List of Contributors


Role of Distal Residues in Structure, Ligand Binding, and Oxidation of Hemoglobins A, Zurich, and Sydney

Properties and Reaction Mechanism of Hb Zurich (α2β2→HIS(63) → ARG)

Ligand Binding to Hemoglobins: Effects of Globin Structure

Functional Abnormalities of Whole Blood in Sickle Cell Anemia

Hemostatic Alterations in Sickle Cell Anemia

Assessment of the Clinical Severity of Sickle Cell Disease

Location of the Heme Iron Atoms and Characterization of the Quaternary Structure of the Carbonmonoxy-β4 Tetramer

Hemoglobin Engineering: Consequences of Alterations at Functionally Sensitive Sites Particularly Susceptible to Chemical or Enzymatic Attack

The Oxygen Binding in Abnormal Cobalt Myoglobins and Hemoglobins (Discussion only)

Amino Acids and Peptides as Inhibitors of Sickle Hemoglobin Gelation

Effect of DBA on Hemoglobin SS Cells and Hemoglobin Biosynthesis

Progress in the Natural History Studies of the Clinical Severity of Sickle Cell Disease: Epidemiologic Aspects

Intermolecular Interactions in Crystals of Human Deoxy Hemoglobins A, C, F, and S

Proton Nuclear Magnetic Resonance Studies of Sickle Cell Hemoglobin

Areas of Interaction in the HbS Polymer

Glycosylated Hemoglobins

Glycosylation of Human Hemoglobin

Evaluation of the Pool of a Hemoglobin Chains and Study of the Dissociation of the Hemoglobin Molecule into Monomers

Inhibition of Sickling by Cystamine

Progress in Interpreting the Phase Transitions of Sickle-Cell Hemoglobin

Circular Dichroism Probes of Hemoglobin Structure

Conformational Effects of the HbS Mutation

Electron Microscopy of Fibers and Crystals of a Deoxygenated Platinum Derivative of Hemoglobin S

Optical Detection of Heme Ligand Configuration in Sperm Whale Myoglobin

The Role of Spectrin and Actin in Irreversibly Sickled Cells: Unsickling of "Irreversibly" Sickled Ghosts by Conditions Which Interfere with Spectrin-Actin Polymerization

Spectrin Assembly in Irreversibly Sickled Cell Membranes: Role of Calcium and ATP

Hemoglobin Interactions and Whole Blood Oxygen Equilibrium Curves in Sickling Disorders

Determination of the Structure of the Fibers of Hemoglobin S by Electron Microscopy and Three-Dimensional Image Reconstruction

Functional Identity of Hemoglobins S and A in the Absence of Polymerization

The Apparent Absence of a Ligand-Linked Structural Transition in the Region of the ß6 Valine of Hemoglobin S

Ligand Binding and the Gelation of Sickle Cell Hemoglobin

Successes and Failures of a Simple Nucleation Theory for Sickle Cell Hemoglobin Gelation

Redox System: iron(II)-iron(III) Interconversion in Oxygen-Carrying Proteins

Mechanisms for Hemoglobin Oxidation: The Response of Abnormal Human and Other Hemoglobins to Different Oxidative Pathways

Oxidation of Oxyhemoglobin by Reductants

Crossings Over versus Point Mutations as Causes of Hemoglobin Variants and Possibly of Thalassemias

Hemoglobin and the Red Cell Membrane

Structural Aspects of Hemoglobin Function

Effects of Heme Iron Ligands on Self-Association of ßSH Chains

Allosteric Binding Heat Effects of HbA and HbM Iwate

Analysis of Oxygen Equilibria in Synthetic and Natural Mutant Valence Hybrid Hemoglobins: Implications for Models of Heme-Heme Interaction in Normal Hemoglobin

The Kinetics of Oxygen Binding to Human Red Blood Cells

Measurement of Homeostatic Responses to Altered P50 in Patients with Abnormal Hemoglobins

Oxidation of Human Hemoglobin by Copper: Specificity for Beta Chains and Formation of Modified Precursor

Dichloromethane as an Antisickling Agent in Sickle Cell Hemoglobin

Fourier Transform Infrared Spectroscopy of Hemoglobin

A Comparative EPR Study of Hemoglobins A and Kansas: Spectral Signatures of Affinity States

Ionic and Non-Ionic Effects on the Solubility of Deoxyhemoglobin S

Anionic Control of Hemoglobin Function

Inhibition of Erythrocyte Sickling in Vitro by Glyceraldehyde

Major Sites for the Oxygen-Linked Binding of Chloride to Hemoglobin

Effectors of the Rate of Deoxyhemoglobin S Polymerization



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© Academic Press 1978
1st January 1978
Academic Press
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About the Editor

Winslow Caughey

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