Fibrinogen Cordoba I: A gammaArg 275 His substitution associated with defective polymerization

GUGLIELMONE, HUGO; MINOLDO S; JARCHUM GD; ABATE DAGA, DANIEL; BOCCO JOSE LUIS

THROMBOSIS RESEARCH

Elsevier

Lugar: Orlando - USA; Año: 2007 vol. 121 p. 429 - 429

0049-3848

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt">Human fibrinogen (Fg) is a 340 kDa glycoprotein and is composed of three pairs of similar but not identical disulfide-bound polypeptides known as A?¿, B?À, and ?Á chains [1,2]. The?Á chain contains several sites that are crucial for normal fibrin polymerization, including the �ga�h polymerization site which aligns the fibrin monomers into half-staggered protofibrils; the D:D interface which is necessary for proper end-to-end alignment of fibrin molecules in polymers assembling; a high-affinity calcium binding and, activated factor XIII cross-linking sites which catalyzes the formation of ?Á-dimers by i