Dissociation of the subunit structure of fibrin stabilizing factor during activation of the zymogen
L Lorand, AJ Gray, K Brown, RB Credo… - Biochemical and …, 1974 - Elsevier
L Lorand, AJ Gray, K Brown, RB Credo, CG Curtis, RA Domanik, P Stenberg
Biochemical and Biophysical Research Communications, 1974•ElsevierCalcium ions play an essential role in the zymogenic conversion of the fibrin stabilizing
factor (FSF; Factor XIII of plasma) in that they cause a dissociation of the two types of
subunits (a′ from b) of the thrombin-activated factor (FSF′). Disc gel electrophoresis
carried out under non-denaturating conditions and utilizing a newly developed fluorescent
activity staining procedure is eminently suited for demonstrating changes in the quaternary
structure of this protein. Also, kinetic evidence is presented to show that the b type of subunit …
factor (FSF; Factor XIII of plasma) in that they cause a dissociation of the two types of
subunits (a′ from b) of the thrombin-activated factor (FSF′). Disc gel electrophoresis
carried out under non-denaturating conditions and utilizing a newly developed fluorescent
activity staining procedure is eminently suited for demonstrating changes in the quaternary
structure of this protein. Also, kinetic evidence is presented to show that the b type of subunit …
Summary
Calcium ions play an essential role in the zymogenic conversion of the fibrin stabilizing factor (FSF; Factor XIII of plasma) in that they cause a dissociation of the two types of subunits (a′ from b) of the thrombin-activated factor (FSF′). Disc gel electrophoresis carried out under non-denaturating conditions and utilizing a newly developed fluorescent activity staining procedure is eminently suited for demonstrating changes in the quaternary structure of this protein. Also, kinetic evidence is presented to show that the b type of subunit, though enzymatically inactive, plays a role in regulating the rate of the calcium dependent activation of the zymogen.
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