메뉴 건너뛰기




Volumn 30, Issue 12, 1998, Pages 1337-1344

Effects of 6-aminonicotinamide on levels of soluble proteins and enzyme activities in various tissues of Japanese quail

Author keywords

6 Aminonicotinamide; Enzyme activity; Japanese quail; Soluble proteins

Indexed keywords

6 AMINONICOTINAMIDE; ACETYLCHOLINESTERASE; ACID PHOSPHATASE; ADENOSINE TRIPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE; ISOCITRATE DEHYDROGENASE; MALATE DEHYDROGENASE (DECARBOXYLATING); NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032422788     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(98)00102-2     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 0000281046 scopus 로고
    • Inhibition of NADP dependent oxidoreductases by the 6-aminonicotinamide analogue of NADP
    • E. Kohler, H.J. Barrach, D. Neubert, Inhibition of NADP dependent oxidoreductases by the 6-aminonicotinamide analogue of NADP, FEBS Lett. 6 (1970) 225-228.
    • (1970) FEBS Lett. , vol.6 , pp. 225-228
    • Kohler, E.1    Barrach, H.J.2    Neubert, D.3
  • 2
    • 0017158974 scopus 로고
    • Decreased GABA and glutamate concentration in rat brain after treatment with 6-aminonicotinamide, Naunyn-Schmiedebergs
    • L. Bielicki, J. Krieglstein, Decreased GABA and glutamate concentration in rat brain after treatment with 6-aminonicotinamide, Naunyn-Schmiedebergs Arch. Pharmacol. 294 (1976) 157-160.
    • (1976) Arch. Pharmacol. , vol.294 , pp. 157-160
    • Bielicki, L.1    Krieglstein, J.2
  • 3
    • 84933386296 scopus 로고
    • Der kohlenhydratstoffwechsel des gehirns nach blockade des pentose-phosphat-weges durch 6-aminonicotinamide, Hoppe-Seylers
    • K. Lange, H. Kolbe, K. Keller, H. Herken, Der kohlenhydratstoffwechsel des gehirns nach blockade des pentose-phosphat-weges durch 6-aminonicotinamide, Hoppe-Seylers Z. Physiol. Chem. 351 (1970) 1241-1252.
    • (1970) Z. Physiol. Chem. , vol.351 , pp. 1241-1252
    • Lange, K.1    Kolbe, H.2    Keller, K.3    Herken, H.4
  • 4
    • 0000466412 scopus 로고
    • Pyridine nucleotide metabolism: Mechanism of action of the niacin antagonist, 6-aminonicotinamide
    • L. Dietrich, I.M. Friedland, L.A. Kaplan, Pyridine nucleotide metabolism: mechanism of action of the niacin antagonist, 6-aminonicotinamide, J. Biol. Chem. 233 (1958) 964-968.
    • (1958) J. Biol. Chem. , vol.233 , pp. 964-968
    • Dietrich, L.1    Friedland, I.M.2    Kaplan, L.A.3
  • 5
    • 0020427786 scopus 로고
    • The effects of inhibition of hexose monophosphate shunt on the metabolism of glucose and function in rat brain in vivo
    • M.K. Gaitonde, G.M. Evans, The effects of inhibition of hexose monophosphate shunt on the metabolism of glucose and function in rat brain in vivo, Neurochem. Res. 7 (1982) 1163-1179.
    • (1982) Neurochem. Res. , vol.7 , pp. 1163-1179
    • Gaitonde, M.K.1    Evans, G.M.2
  • 6
    • 0016274403 scopus 로고
    • Histochemical changes in the rat spinal cord after exposure to 6-aminonicotinamide
    • J.R. Iglesias-Rozas, R.E. Iglesias, Histochemical changes in the rat spinal cord after exposure to 6-aminonicotinamide, Acta Neuropathol. 28 (1974) 223-232.
    • (1974) Acta Neuropathol. , vol.28 , pp. 223-232
    • Iglesias-Rozas, J.R.1    Iglesias, R.E.2
  • 7
    • 0018255160 scopus 로고
    • Effect of 6-aminonicotinamide on the growth and acetylcholinesterase activity during the differentiation of neuroblastoma cells in vitro, Naunyn-Schmiedebergs
    • M. Zeitz, K. Lange, K. Keller, H. Herken, Effect of 6-aminonicotinamide on the growth and acetylcholinesterase activity during the differentiation of neuroblastoma cells in vitro, Naunyn-Schmiedebergs Arch. Pharmacol. 305 (1978) 117-121.
    • (1978) Arch. Pharmacol. , vol.305 , pp. 117-121
    • Zeitz, M.1    Lange, K.2    Keller, K.3    Herken, H.4
  • 8
    • 0019463834 scopus 로고
    • Glucose utilization in the central nervous system in the acute gliopathy due to 6-aminonicotinamide
    • I.R. Griffiths, P.A. Kelley, J.J. Grome, Glucose utilization in the central nervous system in the acute gliopathy due to 6-aminonicotinamide, Lab. Invest. 44 (1981) 547-552.
    • (1981) Lab. Invest. , vol.44 , pp. 547-552
    • Griffiths, I.R.1    Kelley, P.A.2    Grome, J.J.3
  • 9
    • 0002884373 scopus 로고
    • Effects of antimetabolite 6-aminonicotinamide on carbohydrate, nucleotide and catecholamine metabolism, Korean
    • H.K. Jung, I.K. Park, Effects of antimetabolite 6-aminonicotinamide on carbohydrate, nucleotide and catecholamine metabolism, Korean J. Zool. 35 (1992) 23-28.
    • (1992) J. Zool. , vol.35 , pp. 23-28
    • Jung, H.K.1    Park, I.K.2
  • 10
    • 0019833220 scopus 로고
    • Alternative pathways of glucose utilization in the brain; changes in the pattern of glucose utilization in brain resulting from treatment of rats with 6-aminonicotinamide
    • J.S. Hothersall, M.P. Zubariru, A.L. Greenbaum, Alternative pathways of glucose utilization in the brain; changes in the pattern of glucose utilization in brain resulting from treatment of rats with 6-aminonicotinamide, J. Neurochem. 37 (1981) 1484-1489.
    • (1981) J. Neurochem. , vol.37 , pp. 1484-1489
    • Hothersall, J.S.1    Zubariru, M.P.2    Greenbaum, A.L.3
  • 11
    • 0018874091 scopus 로고
    • Correlated changes in neural cerebral rat brain RNA synthesis by 6-aminonicotinamide
    • E. Knoll-Kohler, F. Wonjnorowicz, H.J. Sarkander, Correlated changes in neural cerebral rat brain RNA synthesis by 6-aminonicotinamide, Exp. Brain Res. 38 (1980) 173-179.
    • (1980) Exp. Brain Res. , vol.38 , pp. 173-179
    • Knoll-Kohler, E.1    Wonjnorowicz, F.2    Sarkander, H.J.3
  • 12
    • 0022411145 scopus 로고
    • Effects of 6-aminonicotinamide on cell growth, poly(ADP-ribose) synthesis and nucleotide metabolism
    • D. Hunting, B. Gowans, J.F. Henderson, Effects of 6-aminonicotinamide on cell growth, poly(ADP-ribose) synthesis and nucleotide metabolism, Biochem. Pharmacol. 34 (1985) 3999-4003.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3999-4003
    • Hunting, D.1    Gowans, B.2    Henderson, J.F.3
  • 13
    • 0022380123 scopus 로고
    • Effects of neonatal treatment with 6-aminonicotinamide on basal and isoproterenol-stimulated ornithine decarboxylase activity in cerebellum of the developing rat
    • G. Morris, J.V. Nadler, C.B. Nemeroff, T.A. Slotkin, Effects of neonatal treatment with 6-aminonicotinamide on basal and isoproterenol-stimulated ornithine decarboxylase activity in cerebellum of the developing rat, Biochem. Pharmacol. 34 (1985) 3281-3284.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3281-3284
    • Morris, G.1    Nadler, J.V.2    Nemeroff, C.B.3    Slotkin, T.A.4
  • 14
    • 0003443850 scopus 로고
    • H.U. Bergmeyer (Ed.), Verlag Chimie Weinheim, Academic Press, New York
    • M. Klingenberg, in: H.U. Bergmeyer (Ed.), Methods of Enzymatic Analysis, vol. VII, Verlag Chimie Weinheim, Academic Press, New York, 1983.
    • (1983) Methods of Enzymatic Analysis , vol.7
    • Klingenberg, M.1
  • 16
    • 77049152954 scopus 로고
    • Further studies on the properties and assay of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver
    • G.E. Clock, P. McLean, Further studies on the properties and assay of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver, Biochem. J. 55 (1953) 400-418.
    • (1953) Biochem. J. , vol.55 , pp. 400-418
    • Clock, G.E.1    McLean, P.2
  • 18
    • 0014512167 scopus 로고
    • Multiple molecular forms of avian aldolase. I. Crystallization and physical properties of chicken (Callus domeslcus) breast muscle aldolase
    • R.R. Marquardt, Multiple molecular forms of avian aldolase. I. Crystallization and physical properties of chicken (Callus domeslcus) breast muscle aldolase, Can. J. Biochem. 47 (1969) 517-526.
    • (1969) Can. J. Biochem. , vol.47 , pp. 517-526
    • Marquardt, R.R.1
  • 19
    • 0000834472 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase
    • P.D. Boyer, H. Lardy, K. Myrback (Eds.), Academic Press, New York
    • S.F. Velick, Glyceraldehyde-3-phosphate dehydrogenase, in: P.D. Boyer, H. Lardy, K. Myrback (Eds.), The Enzymes, vol. 7, Academic Press, New York, 1961, p. 243.
    • (1961) The Enzymes , vol.7 , pp. 243
    • Velick, S.F.1
  • 20
    • 0017234477 scopus 로고
    • Lactate dehydrogenase and isoenzyme changes in rats with experimental thiamine deficiency
    • Y. Hirota, E.M. Cohen, O.H.L. Bing, Lactate dehydrogenase and isoenzyme changes in rats with experimental thiamine deficiency, Metabolism 25 (1976) 1-8.
    • (1976) Metabolism , vol.25 , pp. 1-8
    • Hirota, Y.1    Cohen, E.M.2    Bing, O.H.L.3
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding, Anal. Biochem. 72 (1876) 248-254.
    • (1876) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0345002719 scopus 로고
    • Changes in pentose nucleic acid content of subcellular fractions of brain of the rat during metrazol convulsions
    • G.P. Talwar, B. Sadasivudu, V.C. Chitre, Changes in pentose nucleic acid content of subcellular fractions of brain of the rat during metrazol convulsions, Nature (London) 191 (1961) 1007-1008.
    • (1961) Nature (London) , vol.191 , pp. 1007-1008
    • Talwar, G.P.1    Sadasivudu, B.2    Chitre, V.C.3
  • 27
    • 0025899366 scopus 로고
    • Effects of niacin deficiency on the relative turnover rates of proteins in var-ious tissues of Japanese quail
    • I.K. Park, S. Shin, R.R. Marquardt, Effects of niacin deficiency on the relative turnover rates of proteins in var-ious tissues of Japanese quail, Int. J. Biochem. 23 (1991) 1005-1012.
    • (1991) Int. J. Biochem. , vol.23 , pp. 1005-1012
    • Park, I.K.1    Shin, S.2    Marquardt, R.R.3
  • 28
    • 0010323645 scopus 로고    scopus 로고
    • Effects of 3-acetylpyridine on levels of soluble proteins and enzyme activities in various tissues of Japanese quail
    • J.Y. Kim, S. Shin, I.K. Park, Effects of 3-acetylpyridine on levels of soluble proteins and enzyme activities in various tissues of Japanese quail, Int. J. Biochem. Cell Biol. 30 (1998), 487-495.
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 487-495
    • Kim, J.Y.1    Shin, S.2    Park, I.K.3
  • 30
    • 0013988578 scopus 로고
    • Untersuchungen zum mechanismus zentralnervosas functionsstorungen durch 6-aminonicotinamid, Naunyn Schmiedebergs
    • H. Coper, H. Hadass, H. Lison, Untersuchungen zum mechanismus zentralnervosas functionsstorungen durch 6-aminonicotinamid, Naunyn Schmiedebergs Arch. Pharmacol. 255 (1966) 97-106.
    • (1966) Arch. Pharmacol. , vol.255 , pp. 97-106
    • Coper, H.1    Hadass, H.2    Lison, H.3
  • 31
    • 0032146297 scopus 로고    scopus 로고
    • Effects of niacin deficiency on levels of soluble proteins and enzyme activities in various tissues of Japanese quail
    • Y.H. Koh, K.H. Choi, I.K. Park, Effects of niacin deficiency on levels of soluble proteins and enzyme activities in various tissues of Japanese quail, Int. J. Biochem. Cell Biochem. 30 (1998), 943-953.
    • (1998) Int. J. Biochem. Cell Biochem. , vol.30 , pp. 943-953
    • Koh, Y.H.1    Choi, K.H.2    Park, I.K.3
  • 32
    • 0023131504 scopus 로고
    • Phenobarbital and 6-aminonicotinamide effect on cerebral enzymatic activities related to energy metabolism in different rat brain areas
    • F. Marzatico, F. Dagani, D. Curti, G. Benzi, Phenobarbital and 6-aminonicotinamide effect on cerebral enzymatic activities related to energy metabolism in different rat brain areas, Neurochem. Res. 12 (1987) 33-39.
    • (1987) Neurochem. Res. , vol.12 , pp. 33-39
    • Marzatico, F.1    Dagani, F.2    Curti, D.3    Benzi, G.4
  • 33
    • 0019239355 scopus 로고
    • Estimation of creatine phosphokinase and hydroxyproline in the developing limb: Its use in evaluating the effect of teratogens on myogenesis and chondrogenesis
    • T.E. Kwasigroch, D. Neubert, Estimation of creatine phosphokinase and hydroxyproline in the developing limb: its use in evaluating the effect of teratogens on myogenesis and chondrogenesis, Teratogenesis Carcinogenesis Mutagen 1 (1980) 181-191.
    • (1980) Teratogenesis Carcinogenesis Mutagen , vol.1 , pp. 181-191
    • Kwasigroch, T.E.1    Neubert, D.2
  • 34
    • 0028882669 scopus 로고
    • Effect of prolonged starvation on the activities of muscle enzyme and acetylcholinesterase in tissues of Japanese quail
    • H.I. Kim, I.K. Park, Effect of prolonged starvation on the activities of muscle enzyme and acetylcholinesterase in tissues of Japanese quail, Int. J. Biochem. Cell Biol. 27 (1995) 1161-1168.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1161-1168
    • Kim, H.I.1    Park, I.K.2
  • 35
    • 0015028902 scopus 로고
    • Synthesis and degradation of liver ribosomal RNA in fed and fasted rats
    • C.O. Enwonwu, R. Stambough, L. Sreemby, Synthesis and degradation of liver ribosomal RNA in fed and fasted rats, J. Nutr. 101 (1971) 337-346.
    • (1971) J. Nutr. , vol.101 , pp. 337-346
    • Enwonwu, C.O.1    Stambough, R.2    Sreemby, L.3
  • 36
    • 0014028209 scopus 로고
    • Turnover of liver ribosomes in fed and fasted rats
    • C.A. Hirsch, H.H. Hiatt, Turnover of liver ribosomes in fed and fasted rats, J. Biol. Chem. 241 (1966) 5936.
    • (1966) J. Biol. Chem. , vol.241 , pp. 5936
    • Hirsch, C.A.1    Hiatt, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.