title: The formation of beta fibrin requires a functional a site.
abstract: We used recombinant fibrinogens in which the a site is disrupted to examine beta-fibrin formation in the absence of a functional a site. Our variants have only b sites available, and they showed no evidence of fibrin polymer formation after cleavage of FpB with venzyme. We conclude that B-b interactions are not strong enough to induce clot formation. Our studies do not rule out the involvement of b in the formation of beta-fibrin, yet they do provide evidence that a is likely to be essential in the formation of beta-fibrin.
authors.affiliation: Department of Pathology and Laboratory Medicine, University of North Carolina, Brinkhaus-Bullitt 603, Chapel Hill, NC 27599-7525, USA.
authors.forename: K A
authors.initials: KA
authors.lastname: Hogan
authors.forename: B
authors.initials: B
authors.lastname: Bolliger
authors.forename: N
authors.initials: N
authors.lastname: Okumura
authors.forename: S T
authors.initials: ST
authors.lastname: Lord
mesh_terms: D005337:Fibrin / Q000096:biosynthesis* / Q000378:metabolism; D005340:Fibrinogen / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D005337:Fibrin; D005340:Fibrinogen