The Oligosaccharide Side Chain on Asn-135 of α-Antithrombin, Absent in β-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by Affecting the Heparin-Induced Conformational Change-Reference-Cited by-同舟云学术

The Oligosaccharide Side Chain on Asn-135 of α-Antithrombin, Absent in β-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by Affecting the Heparin-Induced Conformational Change

Published:1997-06-01 Issue:22 Volume:36 Page:6682-6691
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Turk Boris¹,Brieditis Ingrid¹,Bock Susan C.¹,Olson Steven T.¹,Björk Ingemar¹

Affiliation:

1. Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Box 575, S-751 23 Uppsala, Sweden, Department of Microbiology and Immunology and Sol Sherry Thrombosis Research Center, Temple University Medical School, 3400 North Broad Street, Philadelphia, Pennsylvania 19140, and Center for Molecular Biology of Oral Diseases, University of Illinois at Chicago, 801 South Paulina Street, Chicago, Illinois 60612

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9702492

Reference49 articles.

1. Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation

2. Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135

3. Isolation and partial characterization of two distinct types of antithrombin III from rabbit

4. Carbohydrate structures of glycoproteins and glycolipids as differentiation antigens, tumour-associated antigens and components of receptor systems

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