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Literature DB >> 3663108

Infrared spectroscopy of heparin-cation complexes.

Abstract

Hydrated and partially hydrated films and aqueous solutions of heparin, heparans and N-desulphated preparations of these polymers were studied by near- and fundamental-region-i.r. spectroscopy in the presence of a range of countercations. The results suggest that ion binding is not explicable solely in terms of simple electrostatic theory, and that specific cation effects, and the hydration pattern of the polymer-cation complex need to be taken into account.

Entities: Chemical

Mesh：

Substances：

Year: 1987 PMID： 3663108 PMCID： PMC1147965 DOI： 10.1042/bj2440143

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

8 in total

1. A transformation-dependent difference in the heparan sulfate associated with the cell surface.

Authors: C B Underhill; J M Keller
Journal: Biochem Biophys Res Commun Date: 1975-03-17 Impact factor: 3.575

2. Quantitative isolation of purified acidic glycosaminoglycans from rat skin.

Authors: R H Pearce; J M Mathieson
Journal: Can J Biochem Date: 1967-10

3. Hydration behavior of ionic dextran derivatives.

Authors: K Gekko; H Noguchi
Journal: Macromolecules Date: 1974 Mar-Apr Impact factor: 5.985

4. Mobilization of capillary endothelium in vitro induced by effectors of angiogenesis in vivo.

Authors: G Alessandri; K Raju; P M Gullino
Journal: Cancer Res Date: 1983-04 Impact factor: 12.701

5. Potentiation by calcium ions of the antithrombin III inhibition of thrombin.

Authors: W F Long; F B Williamson
Journal: Biochem Biophys Res Commun Date: 1982-01-29 Impact factor: 3.575

6. A physico-chemical study of heparin. Evidence for a calcium-induced co-operative conformational transition.

Authors: J Boyd; F B Williamson; P Gettins
Journal: J Mol Biol Date: 1980-02-25 Impact factor: 5.469

7. Electrostatic interactions in the heparin-enhanced reaction between human thrombin and antithrombin.

Authors: L C Petersen; M Jørgensen
Journal: Biochem J Date: 1983-04-01 Impact factor: 3.857

8. Effect of zinc on decondensation of human spermatozoa nuclei by heparin.

Authors: R Reyes; V M Magdaleno; O Hernández; A Rosado; N M Delgado
Journal: Arch Androl Date: 1983-05

8 in total

11 in total

1. Heparin-polypeptide interaction. Near-i.r. spectroscopy in an anhydrous dispersant allows the involvement of polymer-associated water to be assessed.

Authors: D Grant; W F Long; F B Williamson
Journal: Biochem J Date: 1991-07-15 Impact factor: 3.857

2. Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry.

Authors: Youjin Seo; Matthew R Schenauer; Julie A Leary
Journal: Int J Mass Spectrom Date: 2011-06-01 Impact factor: 1.986

3. Infrared spectroscopy of heparins suggests that the region 750-950 cm-1 is sensitive to changes in iduronate residue ring conformation.

Authors: D Grant; W F Long; C F Moffat; F B Williamson
Journal: Biochem J Date: 1991-04-01 Impact factor: 3.857

Infrared spectroscopy of heparin-cation complexes.

1. A transformation-dependent difference in the heparan sulfate associated with the cell surface.

2. Quantitative isolation of purified acidic glycosaminoglycans from rat skin.

3. Hydration behavior of ionic dextran derivatives.

4. Mobilization of capillary endothelium in vitro induced by effectors of angiogenesis in vivo.

5. Potentiation by calcium ions of the antithrombin III inhibition of thrombin.

6. A physico-chemical study of heparin. Evidence for a calcium-induced co-operative conformational transition.

7. Electrostatic interactions in the heparin-enhanced reaction between human thrombin and antithrombin.

8. Effect of zinc on decondensation of human spermatozoa nuclei by heparin.

1. Heparin-polypeptide interaction. Near-i.r. spectroscopy in an anhydrous dispersant allows the involvement of polymer-associated water to be assessed.

2. Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry.

3. Infrared spectroscopy of heparins suggests that the region 750-950 cm-1 is sensitive to changes in iduronate residue ring conformation.

4. A potentiometric titration study of the interaction of heparin with metal cations.

5. Cu(2+)-heparin interaction studied by polarimetry.

6. Infrared spectroscopy of chemically modified heparins.

7. A study of Ca(2+)-heparin complex-formation by polarimetry.

8. Zn(2+)-heparin interaction studied by potentiometric titration.

9. Inhibition by heparin of Fe(II)-catalysed free-radical peroxidation of linolenic acid.

Review 10. Tools for the Quality Control of Pharmaceutical Heparin.