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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
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