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January 1, 1992BloodOpen Access

Low molecular weight heparin

J. Hirsh MN Levine

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Key Points

To examine how low molecular weight heparin binds to antithrombin, focusing on its structural components.
Analysis of the pentasaccharide structure of low molecular weight heparin.
Identification of critical sulfation at the third residue for binding efficacy.
Investigated the interaction mechanisms between low molecular weight heparin and antithrombin.
The third residue being 3-O-sulfated glucosamine is essential for effective binding to antithrombin.
Structural analysis confirmed specific molecular requirements for heparin's activity.

Implication

Investigation of low molecular weight heparin’s binding to antithrombin, highlighting its critical molecular structure.

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Cite This Study

Hirsh et al. (1992) studied this question.

synapsesocial.com/papers/6a223c51438af9b5d1a41a8a https://doi.org/10.1182/blood.v79.1.1.1

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Keep reading

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Interaction of heparin and antithrombin IIIOriginal Research · 1988 · 63 citations
2Antithrombin III Geneva: A Hereditary Abnormal AT III with Defective Heparin Cofactor Activitycase_series · 1987 · 10 citations
3Antithrombin III Northwick Park: demonstration of an inactive high MW complex with increased affinity for heparinpreclinical · 1987 · 33 citations
4The In Vitro Effects of Antithrombin III on the Activated Coagulation Time in Patients on Heparin TherapyIn Vitro Study · 2000 · 65 citations
5Comparative Inhibition of Extrinsic and Intrinsic Thrombin Generation by Standard Heparin, a Low Molecular Weight Heparin and the Synthetic ATIII-Binding PentasaccharideIn Vitro Study · 1993 · 27 citations

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