Literature DB >> 6232950

Anticoagulantly active heparin-like molecules from vascular tissue.

J A Marcum, R D Rosenberg.   

Abstract

Mucopolysaccharides were isolated from calf cerebral microvasculature and calf aorta. The only complex carbohydrates that exhibited anticoagulant activity were heparin-like components. The biologic potencies of calf cerebral and aortic heparin-like species were 2.92 units/mg of anti-factor Xa activity and 2.85 units/mg of anti-factor IIa activity, as well as 0.56 unit/mg of anti-factor Xa activity and 0.19 unit/mg of anti-factor IIa activity, respectively. Additional experiments revealed that the anticoagulantly active aortic components were significantly present only within the intima. The above populations of heparin-like species were affinity fractionated with antithrombin. The highly active component obtained from calf cerebral microvasculature exhibited an anti-factor Xa activity of 40.7 units/mg as well as an anti-factor IIa activity of 36.8 units/mg, constituted about 4.2% of the initial mass of the starting material, and represented about 75% of the biologic potency of the starting material. The highly active component derived from calf aorta exhibited an anti-factor Xa activity of 55.4 units/mg as well as an anti-factor IIa activity of 11.3 units/mg, constituted about 0.3% of the initial mass of the starting material, and represented about 60% of the biologic potency of the starting material. The highly active cerebral microvascular species possessed a molecular weight and charge density similar to that of heparan sulfate whereas the highly active aortic species displayed a molecular weight and charge density equivalent to that of a hexadecasaccharide fragment of heparin.

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Year:  1984        PMID: 6232950     DOI: 10.1021/bi00303a023

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  49 in total

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4.  Hemostatic regulation and Whitehead's philosophy of organism.

Authors:  J A Marcum; G M Verschuuren
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5.  Expression and functional characterization of two natural heparin-binding site variants of antithrombin.

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6.  Engineering D-helix of antithrombin in alpha-1-proteinase inhibitor confers antiinflammatory properties on the chimeric serpin.

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Authors:  D Kirchhofer; T B Tschopp; P Hadváry; H R Baumgartner
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8.  Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells.

Authors:  E Ersdal-Badju; A Lu; X Peng; V Picard; P Zendehrouh; B Turk; I Björk; S T Olson; S C Bock
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9.  Detection of glycosaminoglycans on the surface of human umbilical vein endothelial cells using gold-conjugated poly-L-lysine with silver enhancement.

Authors:  N J Klein; G I Shennan; R S Heyderman; M Levin
Journal:  Histochem J       Date:  1993-04

10.  Antithrombin is protective against myocardial ischemia and reperfusion injury.

Authors:  J Wang; Y Wang; J Wang; J Gao; C Tong; C Manithody; J Li; A R Rezaie
Journal:  J Thromb Haemost       Date:  2013-06       Impact factor: 5.824

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