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

1981; Wiley; Volume: 113; Issue: 3 Linguagem: Inglês

10.1111/j.1432-1033.1981.tb05089.x

1432-1033

Faustino Menegus, Mario Pace,

Biochemical and Molecular Research

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 33000 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. crussa grown in a ‘zinc‐deficient’ medium.