The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
The molecular-weight-dependence of the anti-coagulant activity of heparin
Open accessAbstract
It is proposed that the anti-coagulant activity of heparin is related to the probability of finding, in a random distribution of different disaccharides, a dodecasaccharide with the sequence required for binding to antithrombin. It is shown that this probability is a function of the degree of polymerization of heparin. The hypothesis has been been tested with a series of narrow-molecular-weight-range fractions ranging from 5,600 to 36,000. The fractions having mol.wts. below 18,000 (comprising 85% of the original preparation) followed the predicted probability relationship as expressed by the proportion of molecules capable of binding to antithrombin. The probability that any randomly chosen dodecasaccharide sequence in heparin should bind to antithrombin was calculated to 0.022. The fraction with mol.wt. 36,000 contained proteoglycan link-region fragments, which may explain the deviation of the high-molecular-weight fractions from the hypothetical relationship. The relationship between anti-coagulant activity and molecular weight cannot be explained solely on the basis of availability of binding sites for antithrombin. The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight. Possible explanations of this finding are discussed. One explanation could be a requirement for binding of thrombin to the heparin chain adjacent to antithrombin.
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Citations
Cites
A modified uronic acid carbazole reaction
Bitter, T., & Muir, H. M. (1962) · Analytical Biochemistry · doi:10.1016/0003-2697(62)90095-7 · Cited by 6,274
The Purification and Mechanism of Action of Human Antithrombin-Heparin Cofactor
Rosenberg, R. D., & Damus, P. S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43472-8 · Cited by 1,356
Purification and Properties of Bacterial Chondroitinases and Chondrosulfatases
Yamagata, T., Saito, H., Habuchi, O., & Suzuki, S. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93574-x · Cited by 1,236
Aliphatic Ammonium Salts in the Assay of Acidic Polysaccharides from Tissues
Scott, J. E. (1960) · Methods of Biochemical Analysis · doi:10.1002/9780470110249.ch4 · Cited by 678
Anticoagulant Action of Heparin
DAMUS, P. S., HICKS, M., & ROSENBERG, R. D. (1973) · Nature · doi:10.1038/246355a0 · Cited by 547
The separation of active and inactive forms of heparin
Lam, L. H., Silbert, J. E., & Rosenberg, R. D. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90558-1 · Cited by 492
Andersson, L.-O., Barrowcliffe, T. W., Holmer, E., Johnson, E. A., & Sims, G. E. C. (1976) · Thrombosis Research · doi:10.1016/0049-3848(76)90105-5 · Cited by 457
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Self-citationHighly Purified Antithrombin III with Heparin Cofactor Activity Prepared by Disc Electrophoresis
Abildgaard, U. (1968) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365516809076981 · Cited by 275
The Role of Serine in the Linkage of Heparin to Protein
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Self-citation
Cited by
Mechanism of the anticoagulant action of heparin
Bj�rk, I., & Lindahl, U. (1982) · Molecular and Cellular Biochemistry · doi:10.1007/bf00421226 · Cited by 494
Self-citationStructure and Biological Activity of Heparin
Casu, B. (1985) · Advances in Carbohydrate Chemistry and Biochemistry · doi:10.1016/s0065-2318(08)60067-0 · Cited by 428
Structure of the antithrombin-binding site in heparin.
Lindahl, U., Bäckström, G., Höök, M., Thunberg, L., Fransson, L. A., & Linker, A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3198 · Cited by 368
Self-citationAnticoagulant activities of heparin oligosaccharides and their neutralization by platelet factor 4
Lane, D. A., Denton, J., Flynn, A. M., Thunberg, L., & Lindahl, U. (1984) · Biochemical Journal · doi:10.1042/bj2180725 · Cited by 342
Self-citationDesign of Peptides with High Affinities for Heparin and Endothelial Cell Proteoglycans
Verrecchio, A., Germann, M. W., Schick, B. P., Kung, B., Twardowski, T., & San Antonio, J. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7701 · Cited by 102
Metadata
- Authors
- Laurent, T. C., Tengblad, A., Thunberg, L., Höök, M., & Lindahl, U.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1978-11-01
- Volume
- 175
- Issue
- 2
- Pages
- 691-701
- ISSN
- 0264-6021 (ISSN-L)
- OpenAlex
- W1933438817
- Cited by
- 273
- References
- 20
- FWCI
- 13.47
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Laurent, T. C., Tengblad, A., Thunberg, L., Höök, M., & Lindahl, U. (1978). The molecular-weight-dependence of the anti-coagulant activity of heparin. Biochemical Journal. https://doi.org/10.1042/bj1750691
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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