Binding to antithrombin of heparin fractions with different molecular weights
نویسندگان
چکیده
منابع مشابه
The 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 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 کاملMolecular weight analysis of antithrombin III-heparin and antithrombin III-thrombin-heparin complexes.
The molecular interactions between components of the heparin-catalyzed antithrombin III/thrombin reaction were investigated by light scattering. When heparin was added to antithrombin III, the molecular weight increased to a maximum and then decreased to that of a 1:1 (antithrombin III X heparin) complex. The initial molecular weights at low heparin to antithrombin III ratios were consistent wi...
متن کاملOn the Specificity of Heparin/Heparan Sulfate Binding to Proteins. Anion-Binding Sites on Antithrombin and Thrombin Are Fundamentally Different
BACKGROUND The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. The fundamental structural basis for the origin of specificity, or lack thereof, in these interactions remains unclear. The availability of multiple co-crystal structures facilitates a structu...
متن کاملStructure of the antithrombin-binding site in heparin.
Heparin preparations from pig intestinal mucosa and from bovine lung were separated by chromatography on antithrombin-Sepharose into a high-affinity fraction (with high anticoagulant activity) and a low-affinity fraction (with low anticoagulant). Antithrombin-binding heparin fragments (12-16 monosaccharide units) were prepared, either by digesting a high-affinity heparin-antithrombin complex wi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1930427