Zobrazeno 1 - 7
of 7
pro vyhledávání: '"C G Cockburn"'
Publikováno v:
Thrombosis and Haemostasis. 61:378-385
SummaryThe binding of fn to collagen (type I) fibres has been found to resemble that of vWf in the following respects: 1. Binding is rapid, specific, saturable, similar at 4 and 37°C, and reduced by increasing ionic strength.2. Binding is not inhibi
Publikováno v:
Thrombosis and Haemostasis. 40:302-315
SummaryHighly purified factor VIII was incubated for up to 24 hours in the presence of plasmin, and the biological activities and peptide structure of the digestion products determined at intervals. Procoagulant activity (VIIIC) was rapidly lost, but
Publikováno v:
Thrombosis and Haemostasis. 59:186-192
SummaryFollowing fragmentation of the collagen molecule, we have examined the ability of the isolated fragments to bind vWf. In view of the importance of collagen tertiary and quaternary structure for binding, fragments were first renatured to restor
Autor:
C. G. Cockburn
Publikováno v:
VIth International Congress on Thrombosis and Haemostasis.
A dilute solution of highly purified human FVIII was cross-linked by dimethyl suberimidate (negligible intermolecular cross-linking), incubated in 0.2m mercaptoethanol for 35 min. At 37 c, and eluted through a sepharose 4b column. Unreduced SDS-polya
Publikováno v:
Thrombosis and haemostasis. 40(2)
Publikováno v:
Thrombosis and haemostasis. 59(2)
Following fragmentation of the collagen molecule, we have examined the ability of the isolated fragments to bind vWf. In view of the importance of collagen tertiary and quaternary structure for binding, fragments were first renatured to restore tripl
Publikováno v:
VIth International Congress on Thrombosis and Haemostasis.
Purified human factor VIII was incubated for up to 24 hours with plasmin, and the activity of the breakdown products studied at intervals. Factor VIII coagulant activity was lost within the first hour, but von Willebrand factor activity (FVIIIR:WF) w