[Influence of end products of plasmin-mediated hydrolysis of fibrinogen and fibrin (EF and Ef fragments) on fibrinogen cross-linking].
We studied the influence of the end products of plasmin-mediated hydrolysis of fibrinogen and nonstabilized fibrin (EF and Ef fragments) on covalent cross-linking of fibrinogen molecules catalyzed by a fibrin-stabilizing factor (factor XIIIa). The data on elastic and dynamic light scattering reveal no difference in the spatial structure of covalently linked fibrinogen molecules in the presence of the hydrolysis end products EF and Ef. In contrast to the inactive fragment EF, fragment Ef significantly accelerates the enzymatic reaction. This is also confirmed by electrophoresis of the reduced samples indicating a relatively fast accumulation of gamma-dimers and A alpha-polymers as compared to the control samples. Possible molecular mechanisms of this effect are discussed.
Leonova
V B
VB
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 117977 Russia.
Rozenfel'd
M A
MA
Biriukova
M I
MI
Kostanova
E A
EA
Vasil'eva
M V
MV
D000818:Animals; D002417:Cattle; D003432:Cross-Linking Reagents / Q000737:chemistry; D019281:Dimerization; D026122:Factor XIIIa / Q000737:chemistry / Q000378:metabolism; D005337:Fibrin / Q000737:chemistry* / Q000378:metabolism*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry* / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D012542:Scattering, Radiation
D003432:Cross-Linking Reagents; D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C018543:fibrinogen fragment E; D005337:Fibrin; D026122:Factor XIIIa; D005341:Fibrinolysin