[The effect of "aging" of fibrinogen molecule on the structure and properties of fibrin gel].
The effect of molecular "aging" of fibrinogen stimulated by preincubation in solution on the fibrin three-dimensional architecture, its ability to crosslink fibrin-stabilizing factor, and the sensitivity of fibrin gel to plasmin hydrolysis have been studied. The method of elastic light scattering was used to demonstrate that fibrin generated from "defective" fibrinogen had a coarser structure with a higher mean mass-length ratio of polymeric fibers compared to native fibrinogen (2.24 x 10(9) and 1.46 x 10(9) g/(mol x cm), respectively). Crosslinking had no effect on the architecture of both control and experimental fibrin samples. Spectrophotometric and electrophoretic analysis has shown a higher sensitivity of coarse fibrin gels to plasmin. A close correlation between spontaneous local conformational reconstructions in fibrinogen molecule and its functional activity is concluded.
Rozenfel'd
M A
MA
Leonova
V B
VB
Biriukova
M I
MI
D000818:Animals; D002417:Cattle; D005337:Fibrin / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D005341:Fibrinolysin / Q000737:chemistry*; D005782:Gels / Q000737:chemistry; D020836:Protein Structure, Quaternary; D013329:Structure-Activity Relationship; D013997:Time Factors
D005782:Gels; D005337:Fibrin; D005340:Fibrinogen; D005341:Fibrinolysin