Binding of heparin in vitro and in vivo to plasma proteins
Marciniak, E.
Journal of Laboratory and Clinical Medicine 84(3): 344-356
1974
ISSN/ISBN: 0022-2143 PMID: 4368450 Document Number: 3204
Binding to plasma components of heparin at concentrations which are meaningful from the therapeutic standpoint has been investigated. A direct, quantitative method, based on the anticoagulant properties of heparin, gave evidence of both the heparin distribution among plasma fractions and the effect of binding on heparin activity. Hepcirin in vitro and in vivo was found to form molecular complexes with plasma proteins recognizable in Sephadex filtration. Utilizing the method of ultracentrifugation, plasma low-density lipoproteins (LDL) known to couple with heparin at high concentrations were excluded from binding under present experimental conditions. Bound anticoagulant retained its ability to potentiate the inhibitory reaction between antithrombin I ll and coagulation enzymes. Antithrombin Ill was not included into the complex which heparin formed, and no direct binding of heparin to antithrombin Ill in plasma, or to purified antithrombin Ill was observed.
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