Purification of NAD+ glycohydrolase from human serum
dc.contributor.author | Coskun, Ozlem | |
dc.contributor.author | Nurten, Rustem | |
dc.date.accessioned | 2025-01-27T20:53:49Z | |
dc.date.available | 2025-01-27T20:53:49Z | |
dc.date.issued | 2013 | |
dc.department | Çanakkale Onsekiz Mart Üniversitesi | |
dc.description.abstract | In the present study, NAD(+) glycohydrolase was purified from serum samples collected from healthy individuals using ammonium sulfate fractionation, Affi-Gel blue (Cibacron Blue F3GA) affinity chromatography, Sephadex G-100 column chromatography and isoelectric focusing. The final step was followed by a second Sephadex G-100 column chromatography assay in order to remove the ampholytes from the isoelectric focusing step. In terms of enhancement of specific activity, the NAD(+) glycohydrolase protein was purified similar to 480-fold, with a yield of 1% compared with the initial serum fraction. The purified fraction appeared to be homogeneous, with a molecular weight of 39 kDa, as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, and also corresponded to the soluble (monomeric) form of surface antigen CD38. | |
dc.description.sponsorship | Research Fund of the University, Fatih, Istanbul [T-1157/18062001] | |
dc.description.sponsorship | The present study was supported by the Research Fund of the University, Fatih, Istanbul (project T-1157/18062001). | |
dc.identifier.doi | 10.3892/ol.2013.1335 | |
dc.identifier.endpage | 231 | |
dc.identifier.issn | 1792-1074 | |
dc.identifier.issn | 1792-1082 | |
dc.identifier.issue | 1 | |
dc.identifier.pmid | 23946809 | |
dc.identifier.scopus | 2-s2.0-84878276248 | |
dc.identifier.scopusquality | Q2 | |
dc.identifier.startpage | 227 | |
dc.identifier.uri | https://doi.org/10.3892/ol.2013.1335 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12428/25851 | |
dc.identifier.volume | 6 | |
dc.identifier.wos | WOS:000321079100042 | |
dc.identifier.wosquality | Q4 | |
dc.indekslendigikaynak | Web of Science | |
dc.indekslendigikaynak | Scopus | |
dc.indekslendigikaynak | PubMed | |
dc.language.iso | en | |
dc.publisher | Spandidos Publ Ltd | |
dc.relation.ispartof | Oncology Letters | |
dc.relation.publicationcategory | info:eu-repo/semantics/openAccess | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.snmz | KA_WoS_20250125 | |
dc.subject | ADP-ribose | |
dc.subject | affinity chromatography | |
dc.subject | isoelectric focusing | |
dc.subject | NAD glycohydrolase | |
dc.subject | soluble CD38 | |
dc.title | Purification of NAD+ glycohydrolase from human serum | |
dc.type | Article |