Purification and some properties of NAD-glycohydrolase from conidia of Neurospora crassa.
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.
D002846:Chromatography, Affinity; D007526:Isoelectric Point; D008970:Molecular Weight; D009244:NAD+ Nucleosidase / Q000378:metabolism; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology* / Q000254:growth & development
D009244:NAD+ Nucleosidase