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Volumn 18, Issue 1 A, 1998, Pages 263-267

Inhibition of xanthine oxidase by purpurogallin and silymarin group

Author keywords

Antihepatotoxic principle; Antitumor; Phenolic compounds; Purpurogallin; Silymarin group; Xanthine oxidase inhibitors

Indexed keywords

HYPOXANTHINE; PURPUROGALLIN; SILYMARIN; UNCLASSIFIED DRUG; URIC ACID; XANTHINE; XANTHINE OXIDASE; XANTHINE OXIDASE INHIBITOR;

EID: 0031947695     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (28)
  • 1
    • 0027742757 scopus 로고
    • Inhibitory effects of flavonoids on xanthine oxidase
    • Chang WS, Lee YJ, Lu FJ and Chiang HC: Inhibitory effects of flavonoids on xanthine oxidase. Anticancer Res 13: 2165-2170, 1993.
    • (1993) Anticancer Res , vol.13 , pp. 2165-2170
    • Chang, W.S.1    Lee, Y.J.2    Lu, F.J.3    Chiang, H.C.4
  • 3
    • 0028983181 scopus 로고
    • Structure-activity relationship of caffeic acid analogues on xanthine oxidase inhibition
    • Chang WS, Wen PC and Chinag HC: Structure-activity relationship of caffeic acid analogues on xanthine oxidase inhibition. Anticancer Res 15: 703-708, 1995.
    • (1995) Anticancer Res , vol.15 , pp. 703-708
    • Chang, W.S.1    Wen, P.C.2    Chinag, H.C.3
  • 4
    • 0029566975 scopus 로고
    • Structure-activity relationship of coumarins in xanthine oxidase inhibition
    • Chang WS and Chiang HC: Structure-activity relationship of coumarins in xanthine oxidase inhibition. Anticancer Res 15: 1969-1974, 1995.
    • (1995) Anticancer Res , vol.15 , pp. 1969-1974
    • Chang, W.S.1    Chiang, H.C.2
  • 5
    • 0029620516 scopus 로고
    • Inhibitory effects of phenolic carboxylic acid analogues on xanthine oxidase
    • Chang WS, Yan GF and Chiang HC: Inhibitory effects of phenolic carboxylic acid analogues on xanthine oxidase. Anticancer Res 15: 2097-2100, 1995.
    • (1995) Anticancer Res , vol.15 , pp. 2097-2100
    • Chang, W.S.1    Yan, G.F.2    Chiang, H.C.3
  • 6
    • 0028314928 scopus 로고
    • Xanthine oxidase inhibitors from the leaves of Alsophila spinulosa (Hook) Tryon
    • Chiang HC, Lo YJ and Lu FJ: Xanthine oxidase inhibitors from the leaves of Alsophila spinulosa (Hook) Tryon. J Enzyme Inhibit 8(1): 61-71, 1994.
    • (1994) J Enzyme Inhibit , vol.8 , Issue.1 , pp. 61-71
    • Chiang, H.C.1    Lo, Y.J.2    Lu, F.J.3
  • 7
    • 0029960884 scopus 로고    scopus 로고
    • Inhibitory effects of plant growth regulators on xanthine oxidase
    • Sheu SY and Chiang HC: Inhibitory effects of plant growth regulators on xanthine oxidase. Anticancer Res 16: 311-315, 1996.
    • (1996) Anticancer Res , vol.16 , pp. 311-315
    • Sheu, S.Y.1    Chiang, H.C.2
  • 8
    • 0030499352 scopus 로고    scopus 로고
    • Inhibition of xanhtine oxidase by cytokinins and related substances
    • Sheu SY, Lin YC and Chiang HC: Inhibition of xanhtine oxidase by cytokinins and related substances. Anticancer Res 16: 3571-3576, 1996.
    • (1996) Anticancer Res , vol.16 , pp. 3571-3576
    • Sheu, S.Y.1    Lin, Y.C.2    Chiang, H.C.3
  • 9
    • 0030994822 scopus 로고    scopus 로고
    • Inhibition of xanthine oxidase by synthetic cytokinin analogues
    • Sheu SY, Lin YC and Chiang HC: Inhibition of xanthine oxidase by synthetic cytokinin analogues. Anticancer Res 17: 1043-1050, 1997.
    • (1997) Anticancer Res , vol.17 , pp. 1043-1050
    • Sheu, S.Y.1    Lin, Y.C.2    Chiang, H.C.3
  • 10
    • 1842390084 scopus 로고    scopus 로고
    • edited by Langone JJ and Vanakis HV. In: (Halfman CJ ed), Section II. Data analysis. Chapter 32. Concentrations of binding proteins and labeled analyte that are appropriate for measuring at any analyte concentration range in radioimmunoassays.
    • Colowick SP and Kaplan NO: Methods in Enzymology. Vol. 74. Immunochemical Techniques. Part C edited by Langone JJ and Vanakis HV. In: (Halfman CJ ed), Section II. Data analysis. Chapter 32. Concentrations of binding proteins and labeled analyte that are appropriate for measuring at any analyte concentration range in radioimmunoassays. pp. 481-497, and (Ukraincik K and Piknosh W eds), Chapter 33, Microprocessor-based radioimmunoassay data analysis. New York; Academic Press Inc 1981, pp.497-508.
    • Methods in Enzymology. Vol. 74. Immunochemical Techniques , vol.74 , Issue.PART C , pp. 481-497
    • Colowick, S.P.1    Kaplan, N.O.2
  • 11
    • 0019763149 scopus 로고
    • Chapter 33, New York; Academic Press Inc
    • Colowick SP and Kaplan NO: Methods in Enzymology. Vol. 74. Immunochemical Techniques. Part C edited by Langone JJ and Vanakis HV. In: (Halfman CJ ed), Section II. Data analysis. Chapter 32. Concentrations of binding proteins and labeled analyte that are appropriate for measuring at any analyte concentration range in radioimmunoassays. pp. 481-497, and (Ukraincik K and Piknosh W eds), Chapter 33, Microprocessor-based radioimmunoassay data analysis. New York; Academic Press Inc 1981, pp.497-508.
    • (1981) Microprocessor-based Radioimmunoassay Data Analysis , pp. 497-508
    • Ukraincik, K.1    Piknosh, W.2
  • 12
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H and Burk D: The determination of enzyme dissociation constants. J Am Chem Soc 56: 658-666, 1934.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 13
    • 0004217575 scopus 로고
    • Chapter 4. Enzyme. Enzyme inhibition, competitive inhibition; p. 260, uncompetitive inhibition; p. 261, mixed type inhibition. New York, John Wiley and Sons
    • Segel IH: Biochemical Calculations. 2nd ed. In: Chapter 4. Enzyme. Enzyme inhibition, p. 250, competitive inhibition; p. 260, uncompetitive inhibition; p. 261, mixed type inhibition. New York, John Wiley and Sons, 1976.
    • (1976) Biochemical Calculations. 2nd Ed. , pp. 250
    • Segel, I.H.1
  • 14
    • 0030580066 scopus 로고    scopus 로고
    • Molecular structure and antioxidant specificity of purpurogallin in three types of human cardiovascular cells
    • Wu TW, Zeng LH, Fung KP, Richard D Weisel, Andrew Temple and Norman Camerman: Molecular structure and antioxidant specificity of purpurogallin in three types of human cardiovascular cells. Biochem Pharmacol 52: 1073-1080, 1996.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1073-1080
    • Wu, T.W.1    Zeng, L.H.2    Fung, K.P.3    Weisel, R.D.4    Temple, A.5    Camerman, N.6
  • 15
    • 0029874002 scopus 로고    scopus 로고
    • Purpurogallinm inhibits DNA synthesis of murine fibrosarcoma L-929 and U-87MG glioblastoma cell in vitro
    • Fung KP, WU TW and Lui CP: Purpurogallinm inhibits DNA synthesis of murine fibrosarcoma L-929 and U-87MG glioblastoma cell in vitro. Chemotherapy 42: 199-205, 1996.
    • (1996) Chemotherapy , vol.42 , pp. 199-205
    • Fung, K.P.1    Wu, T.W.2    Lui, C.P.3
  • 16
  • 17
    • 0027223398 scopus 로고
    • Purpurogallin, as an antioxidant protector of human erythrocytes against lysis by peroxyl radicals
    • Sugiyama H, Fung KP and Wu TW: Purpurogallin, as an antioxidant protector of human erythrocytes against lysis by peroxyl radicals. Life Sci 53: PL39-43, 1993.
    • (1993) Life Sci , vol.53
    • Sugiyama, H.1    Fung, K.P.2    Wu, T.W.3
  • 18
    • 0028115767 scopus 로고
    • Purpurogallin: In vivo evidence of a novel and effective cardioprotector
    • Wu TW, Wu J, Zeng LH, Au JX, Carey D and Fung KP: Purpurogallin: in vivo evidence of a novel and effective cardioprotector. Life Sei 54: PL23-28, 1994.
    • (1994) Life Sei , vol.54
    • Wu, T.W.1    Wu, J.2    Zeng, L.H.3    Au, J.X.4    Carey, D.5    Fung, K.P.6
  • 19
    • 0003601534 scopus 로고
    • or Aldrich 25492-4
    • th edition. pp.8283, 1976 or Aldrich 25492-4.
    • (1976) th Edition , pp. 8283
  • 20
    • 0026454241 scopus 로고
    • Changes in the xanthine dehydrogenase/ xanthine oxidase ratio in the rat kidney subjected to ischemia-reperfusion stress
    • Sanhueza J, Valdes J, Campos R, Garrido A and Valenzuela A: Changes in the xanthine dehydrogenase/ xanthine oxidase ratio in the rat kidney subjected to ischemia-reperfusion stress. Res Comms in Chem Pathol Pharmacol 78: 211-218, 1992.
    • (1992) Res Comms in Chem Pathol Pharmacol , vol.78 , pp. 211-218
    • Sanhueza, J.1    Valdes, J.2    Campos, R.3    Garrido, A.4    Valenzuela, A.5
  • 21
    • 0017620457 scopus 로고
    • Silymarin- an inhibitor of horseradish peroxidase
    • Greimel A and Koch H: Silymarin- an inhibitor of horseradish peroxidase. Experientia 33: 1417-1418, 1977.
    • (1977) Experientia , vol.33 , pp. 1417-1418
    • Greimel, A.1    Koch, H.2
  • 22
    • 0018592271 scopus 로고
    • Silymarin, an inhibitor of lipoxygenase
    • Fiebrich F and Koch H: Silymarin, an inhibitor of lipoxygenase. Experientia 35: 1548-1550, 1979.
    • (1979) Experientia , vol.35 , pp. 1548-1550
    • Fiebrich, F.1    Koch, H.2
  • 23
    • 0018565423 scopus 로고
    • Silymarin, an inhibitor of prostaglandin synthetase
    • Fiebrich F and Koch H: Silymarin, an inhibitor of prostaglandin synthetase. Experientia 35: 1550-1552, 1979.
    • (1979) Experientia , vol.35 , pp. 1550-1552
    • Fiebrich, F.1    Koch, H.2
  • 24
    • 0344209207 scopus 로고
    • The sensitivity of serum xanthine oxidase and serum glutamic pyruvic transaminase in detecting liver damage
    • Al-Khalidi UAS and Geha RS: The sensitivity of serum xanthine oxidase and serum glutamic pyruvic transaminase in detecting liver damage. Clin Chim Acta 14: 833-835, 1966
    • (1966) Clin Chim Acta , vol.14 , pp. 833-835
    • Al-Khalidi, U.A.S.1    Geha, R.S.2
  • 26
    • 0014606917 scopus 로고
    • A sensitive and nonradioactive assay for serum and tissue xanthine oxidase
    • Ramboer CRH: A sensitive and nonradioactive assay for serum and tissue xanthine oxidase. J Lab and Clin Med 74: 828-835, 1969.
    • (1969) J Lab and Clin Med , vol.74 , pp. 828-835
    • Ramboer, C.R.H.1
  • 27
    • 0021363366 scopus 로고
    • Brain injury, edema and vascular permeability changes induced by oxygen-derived free radicals
    • Chan PH, Schimidley JW, Fishman RA and Longar SM: Brain injury, edema and vascular permeability changes induced by oxygen-derived free radicals. Neurology, 34: 315-320, 1984.
    • (1984) Neurology , vol.34 , pp. 315-320
    • Chan, P.H.1    Schimidley, J.W.2    Fishman, R.A.3    Longar, S.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.