Találati lista | Tudóstér

001-es BibID:	BIBFORM010446
Első szerző:	Lahav, Judith
Cím:	Coagulation factor XIII serves as protein disulfide isomerase / Lahav, J., Karniel, E., Bagoly, Z., Sheptovitsky, V., Dardik, R., Inbal, A.
Dátum:	2009
ISSN:	0340-6245 (Print)
Megjegyzések:	Tissue transglutaminase was reported to act as protein disulfide isomerase (PDI). We studied whether plasma transglutaminase - coagulation factor XIII (FXIII) - has PDI activity as well. PDI activity was measured by determining the ability to renature reduced-denatured RNase (rdRNase). We found that FXIII can renature rdRNase, with efficiency comparable to commercial PDI. This PDI activity was inhibited by bacitracin. Like tissue transglu-taminase, FXIII-mediated PDI activity is independent of its transglutaminase activity and is located on the A subunit. Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation. Our results imply that FXIII-PDI activity may have a role in platelet function.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Factor XIII PDI Transglutaminase bacitracin blood clotting factor 8 integrin nitric oxide protein disulfide isomerase ribonuclease alpha chain article catalysis disulfide bond nitrosation priority journal protein binding protein determination surface property thrombocyte function Animals Antibodies Bacitracin Cattle Enzyme Inhibitors Factor XIII Factor XIIIa Humans Protein Disulfide-Isomerases Protein Renaturation Protein Subunits Ribonuclease Pancreatic
Megjelenés:	Thrombosis and Haemostasis. - 101 : 5 (2009), p. 840-844. -
További szerzők:	Karniel, Eli Bagoly Zsuzsa (1978-) (orvos) Sheptovitsky, Vera Dardik, Rima Inbal, Aida
Internet cím:	elektronikus változat Intézményi repozitóriumban (DEA) tárolt változat DOI
Borító:
Saját polcon: