Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
