메뉴 건너뛰기




Volumn 10, Issue 9, 1997, Pages 978-986

Epitope characterization of malondialdehyde-acetaldehyde adducts using an enzyme-Linked immunosorbent assay

Author keywords

[No Author keywords available]

Indexed keywords

ACETALDEHYDE; ACTIN; ALCOHOL; ALDEHYDE DERIVATIVE; BOVINE SERUM ALBUMIN; EPITOPE; HUMAN SERUM ALBUMIN; LAMININ; MALONALDEHYDE; OVALBUMIN; POLYCLONAL ANTIBODY; POLYLYSINE;

EID: 0030824086     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx970069t     Document Type: Article
Times cited : (63)

References (27)
  • 2
    • 0023573883 scopus 로고
    • Covalent binding of acetaldehyde to proteins: Participation of lysine residues
    • Tuma, D. J., Newman, M. R., Donohue, T. M., and Sorrell, M. F. (1987) Covalent binding of acetaldehyde to proteins: participation of lysine residues. Alcohol. Clin. Exp. Res. 11, 579-584.
    • (1987) Alcohol. Clin. Exp. Res. , vol.11 , pp. 579-584
    • Tuma, D.J.1    Newman, M.R.2    Donohue, T.M.3    Sorrell, M.F.4
  • 4
    • 0002124958 scopus 로고
    • The role of acetaldehyde adducts in liver injury
    • Hall, P., Ed. Edward Arnold, London
    • Tuma, D. J., and Sorrell, M. F. (1995) The role of acetaldehyde adducts in liver injury. In Alcoholic Liver Disease: Pathology and Pathogenesis (Hall, P., Ed.) pp 89-99, Edward Arnold, London.
    • (1995) Alcoholic Liver Disease: Pathology and Pathogenesis , pp. 89-99
    • Tuma, D.J.1    Sorrell, M.F.2
  • 5
    • 0024823493 scopus 로고
    • Role of lipid peroxidation and oxidative stress in alcohol toxicity
    • Cederbaum, A. I. (1989) Role of lipid peroxidation and oxidative stress in alcohol toxicity. Free Radical Biol. Med. 7, 537-539.
    • (1989) Free Radical Biol. Med. , vol.7 , pp. 537-539
    • Cederbaum, A.I.1
  • 6
    • 0021810423 scopus 로고
    • Lipid peroxidation in ethanol poisoning: A critical reconsideration
    • Dianzani, M. U. (1985) Lipid peroxidation in ethanol poisoning: a critical reconsideration. Alcohol Alcohol. 20, 161-173.
    • (1985) Alcohol Alcohol. , vol.20 , pp. 161-173
    • Dianzani, M.U.1
  • 7
    • 0026717172 scopus 로고
    • Increased 4-hydroxynonenal levels in experimental alcoholic liver disease: Association of lipid peroxidation with liver fibrogenesis
    • Kamimura, S., Gaal, K., Britton, R. S., Bacon, B. R., Triadafilopoulus, G., and Tsukamoto, H. (1992) Increased 4-hydroxynonenal levels in experimental alcoholic liver disease: association of lipid peroxidation with liver fibrogenesis. Hepatology 16, 448-453.
    • (1992) Hepatology , vol.16 , pp. 448-453
    • Kamimura, S.1    Gaal, K.2    Britton, R.S.3    Bacon, B.R.4    Triadafilopoulus, G.5    Tsukamoto, H.6
  • 8
    • 0022704180 scopus 로고
    • Properties of conjugated Schiff bases of malondialdehyde
    • Kikugawa, K., and Sugimura, Y. (1986) Properties of conjugated Schiff bases of malondialdehyde. Chem. Pharm. Bull. 34, 1794-1800.
    • (1986) Chem. Pharm. Bull. , vol.34 , pp. 1794-1800
    • Kikugawa, K.1    Sugimura, Y.2
  • 9
    • 0023368715 scopus 로고
    • Involvement of lipid oxidation products in the formation of fluorescent and cross-linked proteins
    • Kikugawa, K., and Beppu, M. (1987) Involvement of lipid oxidation products in the formation of fluorescent and cross-linked proteins. Chem. Phys. Lipids 44, 277-296.
    • (1987) Chem. Phys. Lipids , vol.44 , pp. 277-296
    • Kikugawa, K.1    Beppu, M.2
  • 11
    • 0029125812 scopus 로고
    • Sequential acetaldehyde production, lipid peroxidation, and fibrogenesis in micropig model of alcohol-induced liver disease
    • Niemela, O., Parkkila, S., Yla-Herttuala, S., Villanueva, J., Ruebner, B., and Halsted, C. H. (1995) Sequential acetaldehyde production, lipid peroxidation, and fibrogenesis in micropig model of alcohol-induced liver disease. Hepatology 22, 1208-1214.
    • (1995) Hepatology , vol.22 , pp. 1208-1214
    • Niemela, O.1    Parkkila, S.2    Yla-Herttuala, S.3    Villanueva, J.4    Ruebner, B.5    Halsted, C.H.6
  • 12
    • 0030001945 scopus 로고    scopus 로고
    • Acetaldehyde and malondialdehyde react together to generate distinct protein adducts in the liver during long-term ethanol administration
    • Tuma, D. J., Thiele, G. M., Xu, D. S., Klassen, L. W., and Sorrell, M. F. (1996) Acetaldehyde and malondialdehyde react together to generate distinct protein adducts in the liver during long-term ethanol administration. Hepatology 23, 872-880.
    • (1996) Hepatology , vol.23 , pp. 872-880
    • Tuma, D.J.1    Thiele, G.M.2    Xu, D.S.3    Klassen, L.W.4    Sorrell, M.F.5
  • 13
    • 0017845892 scopus 로고
    • The direct oxidation of ethanol by a catalase- And alcohol dehydrogenase-free reconstituted system containing cytochrome P-450
    • Miwa, G. T., Levin, W., Thomas, P. E., and Lu, A. Y. H. (1978) The direct oxidation of ethanol by a catalase-and alcohol dehydrogenase-free reconstituted system containing cytochrome P-450. Arch. Biochem. Biophys. 30, 464-475.
    • (1978) Arch. Biochem. Biophys. , vol.30 , pp. 464-475
    • Miwa, G.T.1    Levin, W.2    Thomas, P.E.3    Lu, A.Y.H.4
  • 14
    • 0021211838 scopus 로고
    • Studies on peroxidized lipids. V. Formation and characterization of 1,4-dihydropyridine-3,5-dicarbaldehyde as model of fluorescent components in lipofuscin
    • Kikugawa, K., and Ido, Y. (1984) Studies on peroxidized lipids. V. Formation and characterization of 1,4-dihydropyridine-3,5-dicarbaldehyde as model of fluorescent components in lipofuscin. Lipids 19, 600-608.
    • (1984) Lipids , vol.19 , pp. 600-608
    • Kikugawa, K.1    Ido, Y.2
  • 15
    • 0022657550 scopus 로고
    • Subcellular location of secretory proteins retained in the liver during the ethanol-induced inhibition of hepatic protein secretion in the rat
    • Volentine, G. D., Tuma, D. J., and Sorrell, M. F. (1986) Subcellular location of secretory proteins retained in the liver during the ethanol-induced inhibition of hepatic protein secretion in the rat. Gastroenterology 90, 158-165.
    • (1986) Gastroenterology , vol.90 , pp. 158-165
    • Volentine, G.D.1    Tuma, D.J.2    Sorrell, M.F.3
  • 16
    • 0030063987 scopus 로고    scopus 로고
    • Decreased binding of asialoglycoproteins to hepatocytes from ethanol-fed rats. Consequence of both impaired synthesis and inactivation of the asialoglycoprotein receptor
    • Tworek, B. L., Tuma, D. J., and Casey, C. A. (1996) Decreased binding of asialoglycoproteins to hepatocytes from ethanol-fed rats. Consequence of both impaired synthesis and inactivation of the asialoglycoprotein receptor. J. Biol. Chem. 271, 2531-2538.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2531-2538
    • Tworek, B.L.1    Tuma, D.J.2    Casey, C.A.3
  • 17
    • 0000486999 scopus 로고
    • Fluorescent 1,4-dihydropyridines: The malondialdehyde connection
    • Nair, V., Offerman, R. J., Turner, G. A., Pryor, A. N., and Baenziger, N. C. (1988) Fluorescent 1,4-dihydropyridines: the malondialdehyde connection. Tetrahedron 44, 2793-2803.
    • (1988) Tetrahedron , vol.44 , pp. 2793-2803
    • Nair, V.1    Offerman, R.J.2    Turner, G.A.3    Pryor, A.N.4    Baenziger, N.C.5
  • 18
    • 0027310448 scopus 로고
    • Formation of a new 1,1,1 adduct in the reaction of malondialdehyde, n-hexylamine and alkanal under neutral conditions
    • Ohya, T. (1993) Formation of a new 1,1,1 adduct in the reaction of malondialdehyde, n-hexylamine and alkanal under neutral conditions. Biol. Pharm. Bull. 16, 137-141.
    • (1993) Biol. Pharm. Bull. , vol.16 , pp. 137-141
    • Ohya, T.1
  • 21
    • 0018882953 scopus 로고
    • The use of the avidin-biotin complex as a tool in molecular biology
    • Bayer, E. A., and Wilchek, M. (1980) The use of the avidin-biotin complex as a tool in molecular biology. Methods Biochem. Anal. 26, 1-46.
    • (1980) Methods Biochem. Anal. , vol.26 , pp. 1-46
    • Bayer, E.A.1    Wilchek, M.2
  • 22
    • 0007213364 scopus 로고
    • The chemistry of dihydropyridines
    • Eisner, U., and Kuthan, J. (1972) The chemistry of dihydropyridines. Chem. Rev. 72, 1-42.
    • (1972) Chem. Rev. , vol.72 , pp. 1-42
    • Eisner, U.1    Kuthan, J.2
  • 23
    • 0024406375 scopus 로고
    • Acetaldehyde substoichiometrically inhibits bovine neurotubulin polymerization
    • Smith, S. L., Jennett, R. B., Sorrell, M. F., and Tuma, D. J. (1989) Acetaldehyde substoichiometrically inhibits bovine neurotubulin polymerization. J. Clin. Invest. 84, 337-341.
    • (1989) J. Clin. Invest. , vol.84 , pp. 337-341
    • Smith, S.L.1    Jennett, R.B.2    Sorrell, M.F.3    Tuma, D.J.4
  • 24
    • 0026636629 scopus 로고
    • Substoichiometric inhibition of microtubule formation by acetaldehyde-tubulin adducts
    • Smith, S. L., Jennett, R. B., Sorrell, M. F., and Tuma, D. J. (1992) Substoichiometric inhibition of microtubule formation by acetaldehyde-tubulin adducts. Biochem. Pharmacol. 44, 65-72.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 65-72
    • Smith, S.L.1    Jennett, R.B.2    Sorrell, M.F.3    Tuma, D.J.4
  • 25
    • 0023078219 scopus 로고
    • The binding of acetaldehyde to the active site of ribonuclease: Alterations in catalytic activity and effects of phosphate
    • Mauch, T. J., Tuma, D. J., and Sorrell, M. F. (1987) The binding of acetaldehyde to the active site of ribonuclease: alterations in catalytic activity and effects of phosphate. Alcohol Alcohol. 22, 103-112.
    • (1987) Alcohol Alcohol. , vol.22 , pp. 103-112
    • Mauch, T.J.1    Tuma, D.J.2    Sorrell, M.F.3
  • 26
    • 0024325903 scopus 로고
    • Increased covalent binding of acetaldehyde to calmodulin in the presence of calcium
    • Jennett, R. B., Saffari-Fard, A., Sorrell, M. F., Smith, S. L., and Tuma, D. J. (1989) Increased covalent binding of acetaldehyde to calmodulin in the presence of calcium. Life Sci. 45, 1461-1466.
    • (1989) Life Sci. , vol.45 , pp. 1461-1466
    • Jennett, R.B.1    Saffari-Fard, A.2    Sorrell, M.F.3    Smith, S.L.4    Tuma, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.