title: Self-assembly of soluble unlinked and cross-linked fibrin oligomers.
abstract: Self-assembly of soluble unlinked and cross-linked fibrin oligomers formed from desA-fibrin monomer under the influence of factor XIIIa was studied in the presence of non-denaturing urea concentrations. By methods of elastic and dynamic light scattering combined with analytical ultracentrifugation, desA-fibrin oligomers formed in both the presence and absence of the factor XIIIa were shown to be ensembles consisting of soluble rod-like double-stranded protofibrils with diverse weight and size. Unlinked and cross-linked soluble double-stranded protofibrils can reach the length of 350-450 nm. The structure of soluble covalently-linked protofibrils is stabilized by isopeptide γ-dimers. Electrophoretic data indicate a complete absence of isopeptide bonds between α-chains of desA-fibrin molecules. The molecular mechanism of formation of soluble rod-like fibrin structures and specific features of its covalent stabilization under the influence of factor XIIIa are discussed.
authors.affiliation: Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. markrosenfeld@rambler.ru
authors.forename: M A
authors.initials: MA
authors.lastname: Rosenfeld
authors.forename: V B
authors.initials: VB
authors.lastname: Leonova
authors.forename: M I
authors.initials: MI
authors.lastname: Biryukova
authors.forename: M V
authors.initials: MV
authors.lastname: Vasileva
mesh_terms: D026122:Factor XIIIa / Q000737:chemistry*; D005337:Fibrin / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D012995:Solubility; D014461:Ultracentrifugation; D014508:Urea / Q000737:chemistry
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; D011108:Polymers; C011468:fibrinmonomer; D014508:Urea; D005337:Fibrin; D005340:Fibrinogen; D026122:Factor XIIIa