作者: C M Fitzsimmons , C G Cockburn , V Hornsey , C V Prowse , M J Barnes
关键词: Collagen receptor 、 Cyanogen bromide 、 Protein quaternary structure 、 Binding site 、 Biochemistry 、 Von Willebrand factor 、 Collagen Type III 、 Chemistry 、 Fibronectin 、 Type I collagen
摘要: Abstract Following fragmentation of the collagen molecule, we have examined ability isolated fragments to bind vWf. In view importance tertiary and quaternary structure for binding, were first renatured restore triple-helical conformation then polymerized. Results indicate presence specific vWf-binding sites in both alpha 1(I)- 2(I)-chains type I collagen. Cleavage 1(I)-chain with cyanogen bromide suggests at least four (conceivably several more) binding implying a wide distribution along length molecule. Collagen III appears possess similar sites. Chemical modification amino acid residues indicates that interaction involves arginyl carboxyl groups Although between fibronectin fibres also (authors' unpublished results), does not compete vWf fibres.