Binding of heparin to metals.
Cell Biochem Biophys
; 59(3): 171-8, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-20981507
Heparin is a major prophylactic and treatment agent for thrombosis. Structurally, this anticoagulant is a polydisperse, highly negatively charged polysaccharide mixture that contains a variable density of sulfate group substituents per molecule. Previous study has shown that heparin molecules have a high affinity for a wide range of metal ions with varying oxidation states. However, reports in literature on binding of heparin to metals have investigated only a small sampling of heparin-metal ion interactions. Since interaction of heparin with fluid phase and cell surface macromolecules in vivo is dependent on the heparin structure when bound in a metal ion complex, a survey of the physical parameters for heparin binding to metals is imperative. Atomic absorption and spectrophotometry experiments were performed for metal quantification, and in this study, the relative values for affinity constants and number of binding sites for heparin binding to several alkaline, alkaline earth, main group, and transition metals in their most common oxidation states are reported. We found an overall trend for heparin-metal affinity to be Mn(2+) > Cu(2+) > Ca(2+) > Zn(2+) > Co(2+) > Na(+) > Mg(2+) > Fe(3+) > Ni(2+) > Al(3+)> Sr(2+), with the trend in N (b) being opposite compared with the K (a).
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Heparina
/
Elementos de Transição
/
Metais Alcalinos
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Metais Alcalinoterrosos
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article