Heparin with two binding sites for antithrombin or platelet factor 4.
نویسندگان
چکیده
منابع مشابه
Enzymatic preparation of heparin oligosaccharides containing antithrombin III binding sites.
Two new oligosaccharides were prepared from heparin by its partial depolymerization using heparin lyase I (EC 4.2.2.7) in an attempt to prepare oligosaccharides having intact antithrombin III binding sites. The oligosaccharides were purified by chromatography on the basis of both size and charge and demonstrated a high level of purity by capillary electrophoresis. One- and two-dimensional 1H NM...
متن کاملScreening for heparin binding variants of antithrombin.
A chromogenic assay for use as a screening test for the identification of antithrombin deficiency is described. The heparin concentration and the incubation time in the assay were optimised specifically to permit the detection of heparin binding defects of antithrombin. The sensitivity of antithrombin assays for the detection of this type of variant was significantly impaired when an incubation...
متن کاملBinding of anti-platelet factor 4/heparin antibodies depends on the thermodynamics of conformational changes in platelet factor 4.
The chemokine platelet factor 4 (PF4) undergoes conformational changes when complexing with polyanions. This can induce the antibody-mediated adverse drug effect of heparin-induced thrombocytopenia (HIT). Understanding why the endogenous protein PF4 becomes immunogenic when complexing with heparin is important for the development of other negatively charged drugs and may also hint toward more g...
متن کاملThe antithrombin-binding sequence of heparin.
Products obtained by partial depolymerization of pig mucosal heparin with nitrous acid were fractionated by affinity chromatography on immobilized antithrombin. A high affinity octasaccharide fraction was recovered and reduced with sodium [3H]borohydride, yielding terminal 2,5-anhydro-~-[l-~H]mannitol residues. Partial N-desulfation of this material by treatment with aqueous dimethylsulfoxide r...
متن کاملBinding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa.
Because free factor VIIa is inactivated only very slowly by a plasma concentration of antithrombin III (AT III) even in the presence of heparin, it has been assumed that AT III plays no significant role in regulating the initiation of tissue factor-dependent blood coagulation. However, in the present study, we present evidence that factor VIIa bound to tissue factor, unlike free factor VIIa, is...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68378-x