Purification of NAD glycohydrolase from human serum Oncology letters 6 227 231 2013

OpenAlex English

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 ~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.