Purification and some properties of NAD-glycohydrolase from conidia of Neurospora crassa

Eur J Biochem. 1981 Jan;113(3):485-90. doi: 10.1111/j.1432-1033.1981.tb05089.x.


NAD-glycohydrolase from conidia of Neurospora crassa was purified by affinity chromatography, using 4-methylnicotinamide adenine dinucleotide as ligand immobilized onto Sepharose through a hydrophilic spacer arm. The pure enzyme is a glycoprotein with an isoelectric point of 5.5 and a molecular weight of 33 000 as determined by sodium dodecylsulphate gel electrophoresis. The specific activity is the highest so far found for NAD-glycohydrolases and in various aspects the enzyme is different from that isolated from mycelia of N. crassa grown in a 'zinc-deficient' medium.

Publication types

  • Comparative Study

MeSH terms

  • Chromatography, Affinity
  • Isoelectric Point
  • Molecular Weight
  • NAD+ Nucleosidase / metabolism
  • Neurospora / enzymology*
  • Neurospora crassa / enzymology*
  • Neurospora crassa / growth & development


  • NAD+ Nucleosidase