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001-es BibID:	BIBFORM060650
Első szerző:	Jeleńska, Magdalena M.
Cím:	The comparative ability of plasma and tissue transglutaminases to use collagen as a substrate / Magdalena M. Jeleńska, Laszlo Fesüs, Maria Kopeć
Dátum:	1980
ISSN:	0005-2744
Megjegyzések:	Heat denatured type I and type III calf skin collagen were found to be substrates for guinea pig liver transglutaminase (R-glutaminyl-peptide:amine γ-glutamyl-yltransferase, EC 2.3.2.13) but not for active plasma factor XIII (factor XIIIa). Liver transglutaminase was shown to catalyse incorporation of 14C-putrescine into subunits of denatured collagen of both types, cross-linking of the latter into high molecular weight polymers and their co-cross-linking to fibrin and fibrinogen. Factor XIIIa is inactive in these respects. None of these reactions was catalysed by liver transglutaminase and plasma factor XIIIa when nondenatured collagens both soluble or in the forms of reconstituted fibrils served as substrates. Some cross-linking of cleavage products of collagen type I (obtained by treatment with collagenase from human neutrophiles) was induced by liver transglutaminase and factor XIIIa. The results indicate that although appropriate glutamine and lysine residues for a ?-(γ-glutamine) lysine cross-linked formation are present in collagen, the native conformation of collagen prevents the action of liver transglutaminase and factor XIIIa.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Collagen Transglutaminase Plasma Guinea pig liver
Megjelenés:	Biochimica et Biophysica Acta (BBA). Enzymology. - 616 : 2 (1980), p. 167-178. -
További szerzők:	Fésüs László (1947-) (orvos biokémikus) Kopeć, Maria
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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