nicotinamide→Niacinamide→NAD→Glycoside Hydrolases→poly-ADP-ribose

• 15686992(nicotinamide): Quantitation of the niacin metabolites 1-methylnicotinamide and l-methyl-2-pyridone-5-carboxamide in random spot urine samples, by ion-pairing reverse-phase HPLC with UV detection, and the implications for the use of spot urine samples in the assessment of niacin status.

  The assay was applied to the measurement of the niacin status of two subjects using spot urine samples.

• 6215856(Niacinamide): Quantitation of urinary niacin metabolites by reversed-phase liquid chromatography.

  The niacin metabolites N1-methyl-2-pyridone-5-carboxamide (2-PYR) and N1-methylnicotinamide (N-MN) have been quantified in human urine using isocratic reversed-phase high-performance liquid chromatography with ultraviolet detection after a simple anion-exchange clean-up procedure.

• 21194(NAD): Complementary use of the reversed-phase and anion-exchange modes of high-pressure liquid chromatography for studies of reduced nicotinamide adenine dinucleotide.

  The reversed-phase and anion-exchange modes of high-pressure liquid chromatography were used to separate breakdown products and impurities in solutions of the reduced form of nicotinamide adenine dinucleotide (NADH).

• 15802128(Glycoside Hydrolases): Characterization of oxidized nicotinamide adenine dinucleotide (NAD(+)) analogues using a high-pressure-liquid-chromatography-based NAD(+)-glycohydrolase assay and comparison with fluorescence-based measurements.

  A high-pressure-liquid-chromatography (HPLC) - based technique was developed to assess the oxidized nicotinamide adenine dinucleotide (NAD (+)) - glycohydrolase activity of the catalytic domain of Pseudomonas exotoxin A containing a hexa-His tag.

• 6322868(poly-ADP-ribose): [ADP-ribosylation of histones of the chicken liver nucleus at different rates of glycohydrolase hydrolysis of NAD]

  The rate of incorporation of nicotinamide - (adenosine-U-14C) adenine dinucleotide ((Ado-U-14C) NAD) into histones and the poly (ADPR) polymerase activity of chromatin suggest that the NAD-dependent ADP-ribosylation of histones depends on the rate of NAD hydrolysis by glycohydrolase in chicken liver nuclei.