Purification of NAD+ glycohydrolase from human serum

  • Authors:
    • Özlem Coşkun
    • Rüstem Nurten
  • View Affiliations

  • Published online on: May 8, 2013     https://doi.org/10.3892/ol.2013.1335
  • Pages: 227-231
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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 ~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.
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July 2013
Volume 6 Issue 1

Print ISSN: 1792-1074
Online ISSN:1792-1082

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Spandidos Publications style
Coşkun Ö and Coşkun Ö: Purification of NAD+ glycohydrolase from human serum. Oncol Lett 6: 227-231, 2013
APA
Coşkun, Ö., & Coşkun, Ö. (2013). Purification of NAD+ glycohydrolase from human serum. Oncology Letters, 6, 227-231. https://doi.org/10.3892/ol.2013.1335
MLA
Coşkun, Ö., Nurten, R."Purification of NAD+ glycohydrolase from human serum". Oncology Letters 6.1 (2013): 227-231.
Chicago
Coşkun, Ö., Nurten, R."Purification of NAD+ glycohydrolase from human serum". Oncology Letters 6, no. 1 (2013): 227-231. https://doi.org/10.3892/ol.2013.1335