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Volumn 69, Issue 10, 2003, Pages 899-904

Antirheumatoid Arthritis Effect of Rhus verniciflua and of the Active Component, Sulfuretin

Author keywords

Anacardiaceae; Antioxidant; Aurones; Fustin; Rheumatoid arthritis; Rhus verniciflua; Sulfuretin

Indexed keywords

ALDEHYDE OXIDASE; ANTIRHEUMATIC AGENT; C REACTIVE PROTEIN; CATALASE; FREUND ADJUVANT; FUSTIN; GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE; RHUS VERNICIFLUA EXTRACT; SULFURETIN; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; XANTHINE OXIDASE;

EID: 0346216110     PISSN: 00320943     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2003-45097     Document Type: Article
Times cited : (54)

References (24)
  • 1
    • 0038613785 scopus 로고    scopus 로고
    • Effects of climatic factors and tapping date on yield and quality of lactree (Rhus verniciflua) sap
    • Kim MJ, Kim GT, Choi TB, Hyun JO. Effects of climatic factors and tapping date on yield and quality of lactree (Rhus verniciflua) sap. Korean Journal of Plant Resources 1998; 11: 70-9
    • (1998) Korean Journal of Plant Resources , vol.11 , pp. 70-79
    • Kim, M.J.1    Kim, G.T.2    Choi, T.B.3    Hyun, J.O.4
  • 4
    • 0027319441 scopus 로고
    • Copper-dependent antioxidase defenses in inflammatory and autoimmune rheumatic diseases
    • Miesel R, Zuber M. Copper-dependent antioxidase defenses in inflammatory and autoimmune rheumatic diseases. Inflammation 1993; 17: 283-94
    • (1993) Inflammation , vol.17 , pp. 283-294
    • Miesel, R.1    Zuber, M.2
  • 5
    • 0343920420 scopus 로고
    • Total radical-trapping antioxidative capacity of plasma and whole blood chemiluminescence in patients with inflammatory and autoimmune rheumatic diseases
    • Miesel R, Zuber M, Hartung R, Hass R, Kröger H. Total radical-trapping antioxidative capacity of plasma and whole blood chemiluminescence in patients with inflammatory and autoimmune rheumatic diseases. Redox Report 1995; 1: 323-30
    • (1995) Redox Report , vol.1 , pp. 323-330
    • Miesel, R.1    Zuber, M.2    Hartung, R.3    Hass, R.4    Kröger, H.5
  • 9
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissue by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissue by thiobarbituric acid reaction. Analytical Biochemistry 1979; 95: 351-8
    • (1979) Analytical Biochemistry , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 10
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S, Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. European Journal of Biochemistry 1974; 47: 469-74
    • (1974) European Journal of Biochemistry , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 11
    • 0000024078 scopus 로고
    • Catalase
    • (Vergmeyer HU, ed.). Academic Press, New York
    • Aebi H. Catalase. In: Methods of Enzymatic Analysis. (Vergmeyer HU, ed.). Academic Press, New York: 1974: p. 673
    • (1974) Methods of Enzymatic Analysis , pp. 673
    • Aebi, H.1
  • 12
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocytes glutathione peroxidase
    • Paglia ED, Valentine WN. Studies on the quantitative and qualitative characterization of erythrocytes glutathione peroxidase. Journal of Laboratory Clinical Medicine 1967; 70: 158-69
    • (1967) Journal of Laboratory Clinical Medicine , vol.70 , pp. 158-169
    • Paglia, E.D.1    Valentine, W.N.2
  • 13
    • 78651165715 scopus 로고
    • The carbon monoxide binding pigments of liver microsomes: Evidence for its hemoprotein nature
    • Omura T, Sato R. The carbon monoxide binding pigments of liver microsomes: Evidence for its hemoprotein nature. Journal of Biological Chemistry 1964; 239: 2370-85
    • (1964) Journal of Biological Chemistry , vol.239 , pp. 2370-2385
    • Omura, T.1    Sato, R.2
  • 14
    • 0014690734 scopus 로고
    • The regulation of rat liver xanthine oxidase: Conversion in vitro of the enzyme activity from dehydrogenase (Type D) to oxidase (Type O)
    • Stripe F, Della CE. The regulation of rat liver xanthine oxidase: Conversion in vitro of the enzyme activity from dehydrogenase (Type D) to oxidase (Type O). Journal of Biological Chemistry 1969; 244: 3855-63
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 3855-3863
    • Stripe, F.1    Della, C.E.2
  • 16
    • 0020063143 scopus 로고
    • Multiple drug metabolism: p-nitroanisole reversal of acetone enhanced aniline hydroxylation
    • Bidlack WR, Lowery GL. Multiple drug metabolism: p-nitroanisole reversal of acetone enhanced aniline hydroxylation. Biochemical Pharmacology 1982; 31: 311-7
    • (1982) Biochemical Pharmacology , vol.31 , pp. 311-317
    • Bidlack, W.R.1    Lowery, G.L.2
  • 17
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Journal of Biological Chemistry 1953; 55: 416-22
    • (1953) Journal of Biological Chemistry , vol.55 , pp. 416-422
    • Nash, T.1
  • 18
    • 0022575404 scopus 로고
    • Diminished rates of glucuronidation and sulfation in perfused rat liver after chronic ethanol administration
    • Reinke LA, Meyer MJ, Notley KA. Diminished rates of glucuronidation and sulfation in perfused rat liver after chronic ethanol administration. Biochemical Pharmacology 1986; 35: 439-47
    • (1986) Biochemical Pharmacology , vol.35 , pp. 439-447
    • Reinke, L.A.1    Meyer, M.J.2    Notley, K.A.3
  • 19
    • 0016275313 scopus 로고
    • Glutathione S-transferase : The first enzymatic step in mercapturic acid formation
    • Habig WH, Pabist MJ, Jakoby WB. Glutathione S-transferase : The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 1974; 249: 7130-9
    • (1974) Journal of Biological Chemistry , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabist, M.J.2    Jakoby, W.B.3
  • 20
    • 0033800873 scopus 로고    scopus 로고
    • Lipid peroxidation in membranes and low-density lipoproteins: Similarities and differences
    • Sevanian A, Ursini F. Lipid peroxidation in membranes and low-density lipoproteins: similarities and differences. Free Radical Biology and Medicine 2000; 29: 306-11
    • (2000) Free Radical Biology and Medicine , vol.29 , pp. 306-311
    • Sevanian, A.1    Ursini, F.2
  • 21
    • 0034676493 scopus 로고    scopus 로고
    • Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology
    • Mates M. Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology. Toxicology 2000; 153: 83-104
    • (2000) Toxicology , vol.153 , pp. 83-104
    • Mates, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.