The Molecular Basis of Mutant Hemoglobin Dysfunction - 1st Edition - ISBN: 9780444006318, 9781483165219

The Molecular Basis of Mutant Hemoglobin Dysfunction

1st Edition

Editors: Paul B. Sigler
eBook ISBN: 9781483165219
Imprint: North Holland
Published Date: 1st January 1981
Page Count: 352
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The Molecular Basis of Mutant Hemoglobin Dysfunction contains the proceedings of the Comprehensive Sickle Cell Center Symposium on the Molecular Basis of Mutant Hemoglobin Dysfunction held at the University of Chicago, Chicago, Illinois, USA, on 7-10 October 1979. The symposium aims to document the progress of research efforts and bring together biochemists, geneticists, clinicians, counselors, and administrators, so that ensuing research will bring science to bear more effectively on these diseases. The volume contains 31 chapters organized into six sections. Section I presents two papers on the influence of fetal hemoglobin on the risk of complications and ocular manifestations of sickle cell disease. The papers in Section II deal with normal and abnormal gene expression. Section IIII is devoted to the structural analysis of mutant hemoglobins and their aggregates. Section IV focuses on evaluations of the physical and molecular basis of mutant hemoglobin dysfunction. The presentations in Section V cover cell biology and pathophysiology of sickle cell disease. Section VI reviews the status of the therapy of sickle cell disease.

Table of Contents



Plenary Address: Molecular Disease

Section I: Some Clinical Problems Stated for the Molecular Biologist

The Influence of Fetal Hemoglobin on the Risk of Complications of Sickle Cell Anemia

Ocular Manifestations of Sickle Cell Disease

Section II: Expression of Normal and Abnormal Genes

Introductory Remarks

Organization of Normal and Abnormal Human Globin Genes by Restriction Enzyme Analysis

The α-Globin Genotype as a Determinant of Hematologic Parameters in Sickle Cell Trait

Characterization of Linked Human Globin Genes by Molecular Cloning Procedures

Regulation of Human Globin Gene Expression after Gene Transfer

The Introduction of Normal and Mutant Globin Genes into Mammalian Cells Using SV40 Vectors

Section III: Structure Analysis of Mutant Hemoglobins and their Aggregates

Introductory Remarks

Flexibility of the NH2-Terminal Region of the ß Chains of Hemoglobin: Correlation with the Gelation Properties of Deoxyhemoglobin S

Contacts Between Molecular Surfaces in Crystals of Deoxygenated Human Hemoglobins A, C, F, and S

Double Filaments: the Basic Structural Unit of

Deoxygenated Sickle Hemoglobin Fibers

A Plausible Molecular Model for the 14-Filament Fibers of Sickle Cell Hemoglobin

Polymorphic Assemblies of Double Strands of Sickle Cell Hemoglobin and their Role in Fiber and Crystal Formation

The Effect of Additive Conformation on Enhancement of Deoxyhemoglobin Polymerization

Section IV: Molecular Dynamics of Dysfunction and Aggregation

Introductory Remarks

Subunit Assembly and Interactions in Normal and Abnormal Human Hemoglobins

Is It Possible to Deduce the Interaction Between Two Proteins from Their Three-Dimensional Structure?

Peptide Inhibitors of the Gelation of Sickle Hemoglobin

Oxygen Binding and the Gelation of Sickle Cell Hemoglobin

Rheological Properties of the Gelled Phase of Hemoglobin S

Decreased Binding of 2,3-Diphosphoglycerate to Deoxy Hemoglobin S: A Polymerization-Independent Functional Abnormality

Section V: Cell Biology and Pathophysiology of Sickle Cell Disease

Introductory Remarks

Red Cell Membrane Alterations Associated with the Sickling Phenomenon

Sickle Erythrocyte Adherence to Cultured Human Endothelial Cells

Section VI: Prospects for Therapy at the Molecular Level

Introductory Remarks

Prospects for Therapy at the Molecular Level: Historical Review

Covalent Inhibitors of Sickling

Weak Binding Gases as Modulators of Hemoglobin Function

Chemical Modifications of Hemoglobin S at the 2,3-Diphosphoglycerate Binding Site: An Approach to Therapy of Sickle Cell Disease



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© North Holland 1981
North Holland
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About the Editor

Paul B. Sigler

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