SEARCH · PubMed Health

Results for “NICOTINAMIDE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources

PubMed1974

Reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate diaphorase activity in human polymorphonuclear leukocytes.

Total reduced nicotinamide adenine dinucleotide (NADH) and reduced nicotinamide adenine dinucleotide phosphate (NADPH) diaphorase activities were examined in human neutrophils. Approximately two-thirds of each enzyme activity was located in the granule fraction with the remainder in the soluble. The activities in a 27,000 x g supernatant from a sonic extract of human polymorphonuclear leukocytes were characterized. Both NADH and NADPH diaphorase were insensitive to cyanide and azide and showed greater activity at acid pH. K(m) values for nitroblue tetrazolium were not markedly different (33 muM with NADH and 12 muM with NADPH), but there was a 40-fold difference in K(m) for the reduced pyridine nucleotides (10 muM with NADH and 400 muM for NADPH). Since the intracellular concentration of both nucleotides is estimated to be about 50 muM, it is much more likely, from a kinetic argument, that the respiratory burst of phagocytosis is intiated by the oxidation of NADH rather than of NADPH.

Azides↗

PubMed1973

Regulation of the nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenases of Saccharomyces cerevisiae.

Saccharomyces cerevisiae contains two distinct l-glutamate dehydrogenases. These enzymes are affected in a reciprocal fashion by growth on ammonia or dicarboxylic amino acids as the nitrogen source. The specific activity of the nicotinamide adenine dinucleotide phosphate (NADP) (anabolic) enzyme is highest in ammonia-grown cells and is reduced in cells grown on glutamate or aspartate. Conversely, the specific activity of the nicotinamide adenine dinucleotide (NAD) (catabolic) glutamate dehydrogenase is highest in cells grown on glutamate or aspartate and is much lower in cells grown on ammonia. The specific activity of both enzymes is very low in nitrogen-starved yeast. Addition of the ammonia analogue methylamine to the growth medium reduces the specific activity of the NAD-dependent enzyme and increases the specific activity of the NADP-dependent enzyme.

Amino Acids↗

PubMed1975

Nicotinamide adenine dinucleotide levels in chick limb mesodermal cells in vitro: effects of 3-acetylpyridine and nicotinamide.

The studies reported here show that in cultures of developing mesodermal cells, chondrogenic expression is associated with a progressive decline in cellular NAD+ levels. Furthermore, reduced cellular NAD+ levels resulting from exposure to the nicotinamide analog 3-acetylpyridine are correlated with a 2- to 100-fold potentiation of chondrogenic expression. Conversely, elevated NAD+ levels resulting from exposure to nicotinamide alone are correlated with inhibition of chondrogenic expression. These data are consistent with the hypothesis that pyridine nucleotides, or some derivative thereof, play a central role in the control of muscle and cartilage development in embryonic chick limbs.

Animals↗

PubMed1987

[Interaction of muscle glycogen phosphorylase b with nicotinic acid, nicotinamide, N-nicotinyl-gamma-aminobutyric acid and nicotinamide coenzymes].

The inhibitory action of nicotinic acid, nicotinamide, N-nicotinoyl-gamma-aminobutyric acid, NAD, NADH, NADP, and NADPH on the rabbit skeletal muscle glycogen phosphorylase b has been studied. The inhibition is reversible and positively cooperative (the value of Hill coefficients were determined for the following compounds: nicotinic acid (28 mM; 1.4), nicotinamide (4.4 mM; 1.2), N-nicotinoyl-gamma-aminobutyric acid (9.5 mM; 1.4), NAD (4.4 mM; 1.2), NADH (0.93 mM; 1.2). NADH-binding site of glycogen phosphorylase b subunit was characterized by the sedimentation velocity method. Microscopic dissociation constant was found to be 86 +/- 9 microM (pH 6.8; 20 degrees C). AMP-induced association of glycogen phosphorylase b is hindered by NADH.

Animals↗

PubMed1983

Increase of nicotinamide methyltransferase and N1-methyl-nicotinamide oxidase activities in the livers of the rats administered alkylating agents.

Twenty four hours after intraperitoneal injection of alkylating agents, N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), N-methyl-N-nitrosourea (MNU) and methyl methanesulfonate (MMS), into rats, an increase in nicotinamide (Nmd) methyltransferase and N1-methylnicotinamide (1-CH3Nmd) oxidase activities in the liver was found. Since activities of these enzymes in the liver extracts were not stimulated directly by these agents in vitro, it is postulated that the increases in these enzyme activities are due to the induction of each enzyme.

Aldehyde Oxidase↗

PubMed1977

Action of nucleotide phosphotransferase of Escherichia coli on nicotinamide riboside and nicotinamide mononucleotide.

The action of the nucleotide phosphotransferase of Escherichia coli on nicotinamide riboside and on its 5'-phosphate results in the addition of one phosphate moiety to each of the substrates. Although the proof is not conclusive, it is likely that the phosphate group is transferred to the 3'-hydroxyl of the ribose. This is in contrast to the behavior of the enzyme toward NAD in which only the adenylic acid portion is phosphorylated enzymically.

Chemical Phenomena↗

PubMed1976

Application of nicotinamide-adenine dinucleotide analogs for clinical enzymology: a spectrophotometric method for clinical analysis of lactate dehydrogenase patterns with the use of a nicotinamide-adenine dinucleotide analog.

The activities of porcine lactate dehydrogenase (LHD) isoenzymes were analyzed using nicotinamide-adenine dinucleotide (NAD) or its analogs as a cofactor, with varying concentrations of L-lactate from 13 to 530 mM. The greatest differences between H4-type and M4-type isoenzymes in reaction rates were observed when their activities were compared in a reaction mixture containing 530 mM lactate and NAD, and also in a system of 13 mM lactate with thionicotinamide-hypoxanthine dinucleotide as a cofactor. The ratio of the LDH activity exerted in the former reaction mixture to that exerted in the latter was termed the N/T value. The N/T values of porcine H4 and M4 isoenzymes were 0.49 and 9.33, respectively. The N/T values of other three isoenzymes (H3M1, H2M2 and H1M3) were calculated by assuming that the single subunits H1 and M1 contribute one-fourth of the values of 0.49 and 9.33, respectively, and a given isoenzyme which is a combination of four subunits of H and M comprises the sum of their values. The calculated values agreed fairly well with the experimental results. The N/T value method was found to be applicable to human LDH isoenzymes, and sera from various patients were analyzed in comparison with hormonal sera. The method is particularly suitable for the numerical expression of LDH isoenzyme profiles.

Animals↗

PubMed1983

Applicability of the induced-fit model to glyceraldehyde-3-phosphate dehydrogenase from sturgeon muscle. Study of the binding of oxidized nicotinamide adenine dinucleotide and nicotinamide 8-bromoadenine dinucleotide.

A new method of calculation, based on a direct fitting of the protein fluorescence intensity observed upon coenzyme binding (H.-P. Lutz, unpublished results), is used to study the negative cooperative behavior of glyceraldehyde-3-phosphate dehydrogenase from sturgeon muscle. The calculation procedure simultaneously elaborates data obtained for four different protein concentrations, and it is able to compare different models by computing the minimal and critical sum of squares. Using this approach, it is shown that the induced-fit model [Koshland, D. E., Jr., Nemethy, G., & Filmer, D. (1966) Biochemistry 5,365] and the dimer of dimer model [Malhotra, O. P., & Bernhard, S. A. (1968) J. Biol. Chem. 243, 1243-1252] can both be applied for explaining the negative cooperativity observed upon coenzyme binding to sturgeon glyceraldehyde-3-phosphate dehydrogenase. In addition to the progressive modification of the binding affinity during ligand binding, different maximal fluorescence quenchings for the binding steps must be postulated; and furthermore, the binding capability decreases by decreasing the protein concentration. The fact that the induced-fit model can also be applied is rather in contradiction with the view generally accepted of a dimer of dimer structure of sturgeon glyceraldehyde-3-phosphate dehydrogenase. By use of the same approach, nicotinamide 8-bromoadenine dinucleotide is shown to bind to glyceraldehyde-3-phosphate dehydrogenase from sturgeon in a negative cooperative manner.

Animals↗

PubMed2000

Binding of nicotinamide adenine dinucleotide phosphate to the tetratricopeptide repeat domains at the N-terminus of p67PHOX, a subunit of the leukocyte nicotinamide adenine dinucleotide phosphate oxidase.

The nicotinamide adenine dinucleotide phosphate (NADPH) binding site of the NADPH oxidase complex is believed to be located on the beta, subunit of cytochrome b558. However, our previous studies showed that p67PHOX also contains an NADPH binding site that is essential for normal oxidase activity and that p67PHOX is able to mediate a slow electron transfer from a reduced pyridine nucleotide to an artificial electron acceptor. Using both affinity labeling and fluorescence quenching, we have obtained further evidence that p67PHOX is able to bind NADPH. We have used a number of truncated forms of p67PHOX, including p67PHOX(1-243), p67PHOX(1-210), p67PHOX(1-199), and p67PHOX(244-526) (where the numbers represent the initial and final amino acids in the truncated p67PHOX) in order to localize the binding site. We found that NADPH could bind to p67PHOX(1-243), p67PHOX(1-210), and p67PHOX(1-199) but not to p67PHOX(244-526). The p67PHOX(1-199) fragment consists largely of four tetratricopeptide (TPR) domains. We showed further that Rac2-GTP gamma S and to a lesser extent Rac2-GDP beta S could modulate the binding of NADPH to p67PHOX.

Affinity Labels↗

PubMed2000

Lipid peroxidation in nicotinamide-deficient and nicotinamide-supplemented rats.

Supplementation or deficiency of nicotinamide in rats may interfere with the oxidative balance, with excess leading to greater lipid peroxidation, measured by TBARS, and deficiency causing a greater consumption of antioxidants such as vitamin E and glutathione. Urinary N-methylnicotinamide excretion was much more marked in the supplemented group, whereas the difference between deficient and control animals was nonsignificant.

Animals↗

PubMed1966

The requirement for bivalent cations in formation of nicotinamide-adenine dinucleotide by nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei.

1. The requirement for bivalent cations in catalysis of NAD formation from ATP and NMN in the presence of NMN adenylyltransferase of pig-liver nuclei was studied. Rates of NAD formation in the presence of the activating cations Cd(2+), Mn(2+), Mg(2+), Zn(2+), Co(2+) and Ni(2+) were approximately a linear function of heats of hydration of the corresponding ions. Ba(2+), Sr(2+), Ca(2+), Cu(2+) and Be(2+) did not activate the enzyme; Be(2+) inhibited the reaction in the presence of Mg(2+) and, to a greater extent, in the presence of Ni(2+). 2. Michaelis constants for NAD formation, measured in a coupled assay with NMN adenylyltransferase and alcohol dehydrogenase at pH8.0 and 25 degrees , in the presence of 3mm concentrations of the unvaried reactants, were 88+/-7mum-ATP, 42+/-4mum-NMN and 85+/-4mum-Mg(2+). The results at this pH and at pH7.5 were consistent with mechanisms in which Mg(2+)-ATP complex is a reactant and free ATP a competitive inhibitor. 3. Formation of nicotinamide-hypoxanthine dinucleotide from NMN and ITP in the presence of the transferase was also more rapid with Ni(2+) and Co(2+) than with Mg(2+).

Adenosine Triphosphate↗

PubMedDate not supplied

Randomized trial comparing nicotinamide and nicotinamide plus cyclosporin in recent onset insulin-dependent diabetes (IMDIAB 1). The IMDIAB Study Group.

A 1-year open randomized controlled multicentre trial was carried out on 90 patients with recent onset (< 4 weeks) insulin-dependent diabetes (IDDM) to compare the effect of nicotinamide (NCT) with the combination NCT and low dose cyclosporin (CyA) on clinical remission and optimization of metabolic control during the first year from diagnosis. Three groups of patients were randomly assigned to receive for 12 months either NCT 25 mg kg-1 day-1 (n = 30) or NCT 25 mg kg-1 day-1 + CyA 5 mg kg-1 day-1 (n = 30), the latter adjusted to maintain 12 whole blood trough levels of 83 nmol l-1; a third group of patients (n = 30) receiving insulin only acted as a control group for spontaneous remission and metabolic control. Clinical remission (i.e. suspension of insulin therapy with normal metabolic parameters for more than 2 weeks according to the International Diabetes Immunotherapy Group) was achieved at 3 months in 6/30 NCT treated patients and in 1/30 NCT + CyA treated patient (p = 0.05); no remission was observed in control patients. At 6 months the number of patients achieving remission in each group was 4/29, 3/27, and 1/29, respectively (p = NS). One year after diagnosis 4/27 NCT treated, 2/25 NCT+CyA treated but 0/28 of the control patients were in remission (NCT vs control p = 0.05). Clinical remission lasted longer (7 +/- 3 SD months) in NCT treated patients than in NCT+CyA treated or control patients (p < 0.02).(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗

PubMed1969

Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-linked succinic semialdehyde dehydrogenases in a Pseudonomas species.

A Pseudomonas species grown on polyamines was found to have the following enzymes that can dehydrogenate succinic semialdehyde: a constitutive nicotinamide adenine dinucleotide phosphate (NADP)-linked dehydrogenase, an inducible NAD-linked dehydrogenase specific for succinic semialdehyde (EC 1.2.lb), and more than one inducible NAD-linked aminoaldehyde dehydrogenase which can act on succinic semialdehyde, 3-aminopropanal, and 4-aminobutanal. These enzymes have been separated from each other by ammonium sulfate precipitation, column chromatography on diethylaminoethyl-Sephadex, and electrophoresis on polyacrylamide gel. The level of NAD-linked succinic semialdehyde dehydrogenase in cells grown on various C and N sources has been determined and found to be as expected of an inducible enzyme with, however, two slight variations: the basal level of the enzyme in cells grown on Casamino Acids is relatively high and readily detectable, and the level of this enzyme is the same when the cells are grown on gamma-aminobutyrate with or without glucose and is, therefore, not subject to the classical glucose effect.

Aldehydes↗

PubMed1971

Nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lactate dehydrogenases in homofermentative and heterofermentative lactic acid bacteria.

Three homofermentative (Lactobacillus plantarum B38, L. plantarum B33, Pediococcus pentosaceus B30) and three heterofermentative (Leuconostoc mesenteroides 39, L. oenos B70, Lactobacillus brevis) lactic acid bacteria were examined for the presence or absence of nicotinamide adenine dinucleotide (NAD)-dependent and NAD-independent d- and l-lactate dehydrogenases. Two of the six strains investigated, P. pentosaceus and L. oenos, did not exhibit an NAD-independent enzyme activity capable of reducing dichlorophenol indophenol. The pH optima of the lactic dehydrogenases were determined. The NAD-dependent enzymes from homofermentative strains exhibited optima at pH 7.8 to 8.8, whereas values from 9.0 to 10.0 were noted for these enzymes from heterofermentative organisms. The optima for the NAD-independent enzymes were between 5.8 and 6.6. The apparent Michaelis-Menten constants determined for both NAD and the substrates demonstrated the existence of a greater affinity for d- than l-lactic acid. A comparison of the specific NAD-dependent and NAD-independent lactate dehydrogenase activities revealed a direct correlation of the d/l ratios of these activities with the type of lactic acid produced during the growth of the organism.

Ammonium Sulfate↗

PubMed1971

Influence of carboxylic acids on the stereospecific nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lactate dehydrogenases of Leuconostoc mesenteroides.

Leuconostoc mesenteroides increased its lactic acid production from glucose threefold when malic acid was added to the culture. This increase resulted also in a reduction of the ratio of d-lactic acid to l-lactic acid (31.5 to 1.23). Addition of malic acid increased 6.5-fold the specific activity of nicotinamide adenine dinucleotide (NAD)-linked l-lactate dehydrogenase and increased 3.2-fold that of NAD-linked d-lactate dehydrogenase. The Michaelis constant (K(m)) for NAD of the NAD-linked l-lactate dehydrogenase increased with the addition of malate, but no change was observed in the K(m) values for the respective d-enzyme. The effect of carboxylic acids on the NAD-linked l-lactate dehydrogenase activities was tested by using partially purified enzyme preparations from cells grown with glucose alone and from cells grown with glucose plus malate. Malate stimulated the l-enzyme and inhibited the d-lactate dehydrogenase. The NAD-linked l-lactate dehydrogenase exhibited the same activity bands on polyacrylamide gel electrophoresis whether the cell-free preparation originated from cells grown on glucose plus malate or on glucose as the sole carbon source. The NAD-linked d-lactate dehydrogenase, however, exhibited a different pattern of electrophoretic mobility, depending upon the source of origin of the cell-free preparation. The results suggest that malate has a stimulatory effect on the synthesis of both enzymes and may result in rearrangement of the protein structure of the d-lactate dehydrogenase. This rearrangement apparently makes the d-enzyme more susceptible to inhibition of catalytic activity. The l-lactate dehydrogenase, however, is stimulated not only in its synthesis but also in its activity. It is proposed that these effects are responsible for the regulation of lactic acid production.

Acids↗

PubMed1972

Levels of nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide in facultative bacteria and the effect of oxygen.

Nicotinamide adenine dinucleotide (NAD) and reduced NAD (NADH) levels have been measured in bacterial cultures. The cofactors were assayed by using the very sensitive cycling assay described previously by Cartier. Control experiments showed that the level of total NAD(H) falls during harvesting, and so samples were taken quickly from growing cultures and extracted immediately without separating the cells from the medium. Total NAD(H) ranged from 4.0 to 11.7 mumoles/g of dry cells for three facultative organisms, Klebsiella aerogenes, Escherichia coli, and Staphylococcus albus. NADH was remarkably constant in these bacteria; only one out of ten series of determinations was outside the range 1.4 to 1.9 mumoles/g of dry cells. NAD(+) showed much greater variation. An anaerobe (Clostridium welchii) had significantly more total NAD(H) whereas an aerobe Pseudomonas aeruginosa had about as much NAD(H) as the facultative organisms. NAD and NADH were measured during growth: once more NADH was much more constant than NAD. During change-over between aerobiosis and anaerobiosis, NADH showed a temporary increase but then returned to a constant level, whereas NAD changed from high aerobically to low anaerobically. These results are discussed in terms of the control mechanisms that may be involved.

Aerobiosis↗

PubMed1991

Release kinetics of nicotinamide from fatty acid-nicotinamide equimolar complexes. II. Activation thermodynamic quantities.

The rates of release of nicotinamide (NAA) from fatty acid (FA)-NAA complexes, FA-NAA, were determined at various temperatures, and the thermodynamic quantities for the release of NAA were estimated. The results were compared with the previous results obtained for FA-thiamine disulfide (TDS) complexes, (FA)6(TDS). The values of activation enthalpy (delta H ++) and activation entropy (delta S ++) for the release of NAA from FA-NAA were positive and negative, respectively, indicating that the release of NAA is disadvantageous from not only enthalpic but also entropic viewpoints. The plots of delta H++ against the carbon number (n) in the constituent FA showed a zig-zag line with an upward convex at an odd-numbered position and the plots of the absolute values of (-delta S++) showed a zig-zag line with a downward convex at an odd-numbered position, though the positive value of delta H++ increases and the negative value of delta S++ decreases with an increasing n for either even-numbered or odd-numbered FA. It was found that the release of NAA from FA-NAA formed with odd-numbered FA is more disadvantageous enthalpically but more advantageous entropically as compared with that from FA-NAA formed with even-numbered FA. This phenomenon was similar to that observed for (FA)6(TDS). Furthermore, it is suggested that FA-NAA is formed at least by van der Waals forces and hydrophobic interactions and that van der Waals forces are dominant for the formation of FA-NAA formed with odd-numbered FA and that hydrophobic interactions are dominant for the formation of FA-NAA formed with even-numbered FA.

Fatty Acids↗

PubMed1996

Fate of nicotinamide differs due to an intake of nicotinamide.

We found that the catabolism of nicotinamide (Nam) differs due to an intake of Nam itself in rats. When rats were fed with a Nam-free, tryptophan-limiting diet, the major catabolite of niacin was N1-methyl-4-pyridone-3-carboxamide (4-Py). However, its percentage was changed with increasing the intake of Nam. The major metabolite was N1-methylnicotinamide (MNA) in the diet containing 0.006% Nam, or 0.1% Nam. The toxicity of excess Nam was observed when rats were fed with a 0.5% Nam-containing diet. In this diet, the major metabolite was Nam N-oxide and it was noted that the urinary excretion of nicotinic acid and its metabolite nicotinuric acid was observed. Therefore, these acids might be detected only when the toxicity of Nam appears.

Animals↗