The role of conformational domain lability of fibrinogen molecule in the processes of fibrin formation and fibrinolysis.
Rozenfel'd
M A
MA
Emmanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow 117977, Russia.
Leonova
V B
VB
Biryukova
M I
MI
D000818:Animals; D001777:Blood Coagulation; D002417:Cattle; D005337:Fibrin / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry*; D005341:Fibrinolysin / Q000737:chemistry; D005342:Fibrinolysis; D005782:Gels; D007700:Kinetics; D008027:Light; D010958:Plasminogen / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation
D005338:Fibrin Fibrinogen Degradation Products; D005782:Gels; D005337:Fibrin; D005340:Fibrinogen; D010958:Plasminogen; D005341:Fibrinolysin