Biospecific interactions of vitamin K-dependent factors with phospholipid-like polystyrene derivatives. Part II: factor IX.
Biomaterials
; 18(16): 1077-84, 1997 Aug.
Article
em En
| MEDLINE
| ID: mdl-9247344
ABSTRACT
We previously demonstrated that phosphorylated polystyrene derivatives exhibit phospholipid-like behaviour and therefore are able to interact with factor II, one of the vitamin K-dependent coagulation factors. Under the same conditions as for factor II, we examined the interactions of factor IX with phosphorylated resins of various compositions in phosphate groups these studies were carried out with or without albumin precoating of the polymers and either in the presence or absence of calcium ions. Adsorption experiments show that, in the absence of calcium ions, only one class of adsorption sites of factor IX can be evidenced with the interactions taking place through the formation of binary complexes, whereas in the presence of calcium ions, the affinity of factor IX for phosphorylated resins becomes very high and two types of adsorption sites have been evidenced with biospecific ternary complexes being formed. The domains of predominance of these complexes were determined. Moreover, the only functional groups borne by the phosphorylated polystyrene resins involved in factor IX-polymer interactions are phosphodiester groups. Comparison between factor II and factor IX adsorption onto the same polymers leads to the conclusion that the observed differences probably reflect the differences in the Gla domains of the vitamin K-dependent factors. Finally, this study demonstrates that phosphorylated polystyrene derivatives can be used as stationary phases for purification of factor IX by highly specific liquid biochromatography.
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Bases de dados:
MEDLINE
Assunto principal:
Poliestirenos
/
Fator IX
/
Protrombina
Limite:
Humans
Idioma:
En
Revista:
Biomaterials
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
França