Purification and Some Properties of NAD‐Glycohydrolase from Conidia of Neurospora crassa

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Abstract
NAD-glycohydrolase from conidia of N. 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 MW of 33,000 as determined by sodium dodecyl sulfate gel electrophoresis. The specific activity is the highest found for NAD-glycohydrolases and in various aspects the enzyme is different from that isolated from mycelia of N. crassa grown in a Zn-deficient medium.