Human platelet fibrinogen gamma chain structure
نویسندگان
چکیده
منابع مشابه
Human platelet fibrinogen gamma chain structure.
Human plasma fibrinogen is produced by liver parenchymal cells. Such molecules contain two classes of gamma-chains (gamma A, gamma'), which differ with respect to their COOH-terminal sequences. When fibrin is crosslinked in the presence of factor XIIIa and Ca2+, three types of gamma-dimer are formed (gamma A-gamma A; gamma A-gamma'; gamma'-gamma'). A separate fibrinogen pool is located in plate...
متن کاملFibrinogen binding to human blood platelets: effect of gamma chain carboxyterminal structure and length.
Recent evidence suggests that fibrinogen binding to platelets is mediated by the 12 carboxyterminal amino acid residues of the gamma chain. Because human plasma fibrinogen gamma chains differ in mol wt and carboxyterminal amino acid sequence, we examined the effect of such gamma chain heterogeneity on platelet-fibrinogen interactions, using two fibrinogens of distinct composition, separated by ...
متن کاملThree-dimensional structure of the platelet integrin recognition segment of the fibrinogen gamma chain obtained by carrier protein-driven crystallization.
We have developed a method for crystallizing small functional protein segments so that their three-dimensional structure can be determined by x-ray diffraction analysis. This method consists of linking a small protein segment of unknown tertiary structure to either the amino or carboxyl terminus of a larger carrier protein of known tertiary structure. Crystallization of the small segment is the...
متن کاملFibrinogen Gamma Chain Splice Variant γ′ alters Fibrin Formation and Structure
Word Count: 189 Text Word Count: 4,046 Table of
متن کاملHEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Fibrinogen gamma-chain splice variant alters fibrin formation and structure
Fibrinogen A/ results from alternative splicing of mRNA. This variant, which constitutes approximately 8% to 15% of plasma fibrinogen, contains FXIII and thrombin binding sites. Our objective was to investigate whether A/ differs in fibrin formation and structure from the more common variant A/ A. Both variants were separated and purified by anionexchange chromatography. Fibrin formation and cl...
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: Blood
سال: 1984
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v63.5.990.990