Coskun, OzlemNurten, Rustem2025-01-272025-01-2720131792-10741792-1082https://doi.org/10.3892/ol.2013.1335https://hdl.handle.net/20.500.12428/25851In 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.eninfo:eu-repo/semantics/openAccessADP-riboseaffinity chromatographyisoelectric focusingNAD glycohydrolasesoluble CD38Article6122723110.3892/ol.2013.1335Q4WOS:0003210791000422-s2.0-8487827624823946809Q2