Abstract
Abstract NAD was converted chemically to 3-aminopyridine adenine dinucleotide through the Hofmann hypobromite reaction and the resulting dinucleotide was purified by means of ion exchange chromatography. Spectrophotometric and fluorometric properties of the analog were studied. The 3-aminopyridine adenine dinucleotide was shown to be a competitive inhibitor in reactions catalyzed by seven NAD(P)-dependent enzymes. The 3-aminopyridine adenine dinucleotide was diazotized with the use of nitrous acid. The diazotized derivative was shown to be a site-specific inactivator of yeast alcohol dehydrogenase. Diazotized 3-amino-1-methylpyridinium chloride was prepared and shown to be less effective in the inactivation of this enzyme.
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.
