This book describes the complex structures of heparins and heparan sulfates (heparinoids) and how they are generated by their biosynthetic pathways. The book also details the methodologies for studying these structures and their cellular metabolism. Heparin-Binding Proteins introduces the general nature of interactions between heparinoids and proteins, and presents the role for these structures in their interactions with the proteins of the hemostatic mechanisms, fibroblasts growth factors, superoxide dismutase, and lipoproteins.

Key Features

@introbul:Key Features @bul:* Covers cellular metabolism of heparinoid proteoglycans * Written by a distinguished expert in the field of carbohydrate biochemistry * Describes the roles of heparan sulfate proteoglycans in * @subbul:* Blood coagulation and fibrinolysis * Lipoprotein metabolism * Superoxide dismutase activity * Fibroblast growth factor responses of cells


Biochemists and cell biologists; clinicians with an interest in the cardiovascular field.

Table of Contents

Preface. Conventions, Abbreviations, And Terminology. Heparin Vs. Heparan Sulfate. Structures of Heparinoids. Experimental Approaches for Determining Heparinoid Structures. Structural Modification of Heparinoids. The Cellular Metabolism of Heparan Sulfate. Interactions Between Heparinoids and Proteins. Antithrombin: The Prototype for Heparin-Binding Proteins. Heparin-Binding Proteins in Hemostasis. Fibroblast Growth Factors. Extracellular Superoxide Dismutase. Heparin-Binding Proteins in Lipoprotein Metabolism. Epilog. Appendix: Other Heparin-Binding Proteins. Subject Index.


No. of pages:
© 1998
Academic Press
eBook ISBN:
Print ISBN:
Print ISBN:

About the author

H. Conrad

Affiliations and Expertise

School of Chemical Sciences, University of Illinois, Urbana, U.S.A.


"...a remarkable achievement... I found reading this book to be highly rewarding... highly valuable as an introduction to various aspects of heparin/heparan sulfate chemistry and biology." @source:—Ulf Lindahl, Unviersity of Uppsala, Sweden, in JOURNAL OF MEDICINAL CHEMISTRY (1999)