Enzymatic preparation of heparin oligosaccharides containing antithrombin III binding sites (Q38350614)

2 September 2017

Enzymatic preparation of heparin oligosaccharides containing antithrombin III binding sites (English)

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2 September 2017

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5

Linhardt RJ

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2 September 2017

Toida T

1

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2 September 2017

Hileman RE

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2

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2 September 2017

Smith AE

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3

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2 September 2017

Vlahova PI

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4

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2 September 2017

language of work or name

English

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publication date

1 December 1996

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Journal of Biological Chemistry

2 September 2017

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2 September 2017

271

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2 September 2017

50

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2 September 2017

32040-32047

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Heparin: An Old Drug with a New Paradigm

2 September 2017

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Glycosaminoglycans and the regulation of blood coagulation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Anticoagulant activity of heparin: Separation of high‐activity and low‐activity heparin species by affinity chromatography on immobilized antithrombin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Correlation between structure and function of heparin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Structure of the antithrombin-binding site in heparin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-alphs-D-glucopyranoside 3-sulfate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence Chemical and13C nuclear-magnetic-resonance studies

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Structural variation in the antithrombin III binding site region and its occurrence in heparin from different sources

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Structures of five sulfated hexasaccharides prepared from porcine intestinal heparin using bacterial heparinase. Structural variants with apparent biosynthetic precursor-product relationships for the antithrombin III-binding site

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Evaluation of critical groups required for the binding of heparin to antithrombin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Interaction of heparin with synthetic antithrombin III peptide analogues

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Heparin structure and interactions with basic fibroblast growth factor

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Specificity studies on the heparin lyases from Flavobacterium heparinum

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Thermodynamic analysis of heparin binding to human antithrombin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Two-dimensional affinity resolution electrophoresis demonstrates that three distinct heparin populations interact with antithrombin III.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Further characterization of the antithrombin-binding sequence in heparin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Comparative studies on the structures of highly active and relatively inactive forms of whale heparin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Structure and biological activity of finback-whale (Balaenoptera physalus L.) heparin octasaccharide. Chemical, carbon-13 nuclear-magnetic-resonance, enzymic and biological studies

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Preparation and structural characterization of large heparin-derived oligosaccharides

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Microheterogeneity of plasma glycoproteins heparin cofactor II and antithrombin III and their carbohydrate analysis

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Separation of glycosaminoglycan-derived oligosaccharides by capillary electrophoresis using reverse polarity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Substrate specificity of the heparin lyases from Flavobacterium heparinum

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Anticoagulant Activity of Heparin Octasaccharide1

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

Study of structurally defined oligosaccharide substrates of heparin and heparan monosulfate lyases

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.50.32040

21 January 2018

Identifiers

DOI

10.1074/JBC.271.50.32040

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2 September 2017

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