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Volumn 26, Issue 3, 2007, Pages 233-242

Antioxidant actions of phenolic compounds found in dietary plants on low-density lipoprotein and erythrocytes in vitro

Author keywords

Aloe emodin; Anthraquinone derivatives; Barbaloin; Ca2+ ATPase; Erythrocyte membranes; Erythrocytes; Gingerol; Lipid peroxidation; Low density lipoprotein; Na+ K+ ATPase; Oxidative stress; Peroxyl radicals; Protein sulfhydryl groups; Rhapontin; Stilbenes

Indexed keywords

2,2' AZOBIS(2 AMIDINOPROPANE); 6 GINGEROL; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ALOE EMODIN; ALOIN; HEMIN; LOW DENSITY LIPOPROTEIN; PHENOL DERIVATIVE; RHAPONTIN; TERT BUTYL HYDROPEROXIDE; THIOL GROUP; TROLOX C; UNCLASSIFIED DRUG;

EID: 34547180328     PISSN: 07315724     EISSN: 15411087     Source Type: Journal    
DOI: 10.1080/07315724.2007.10719606     Document Type: Article
Times cited : (47)

References (57)
  • 1
    • 0027279233 scopus 로고
    • Prospects for the prevention of free radical disease, regarding cancer and cardiovascular disease
    • Gey KF: Prospects for the prevention of free radical disease, regarding cancer and cardiovascular disease. Br Med Bull 49:679–699, 1993.
    • (1993) Br Med Bull , vol.49 , pp. 679-699
    • Gey, K.F.1
  • 2
    • 21644439609 scopus 로고    scopus 로고
    • Antioxidant nutrients and cancer incident and mortality: An epidemiologic perspective
    • Mayne ST: Antioxidant nutrients and cancer incident and mortality: an epidemiologic perspective. Adv Pharmacol 38:657–675, 1997.
    • (1997) Adv Pharmacol , vol.38 , pp. 657-675
    • Mayne, S.T.1
  • 5
    • 0036774226 scopus 로고    scopus 로고
    • Flavonoid antioxidants: Chemistry, metabolism and structure-activity relationships
    • Heim KE, Tagliaferro AR, Bobilya DJ: Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships. J Nutr Biochem 13:572–584, 2002.
    • (2002) J Nutr Biochem , vol.13 , pp. 572-584
    • Heim, K.E.1    Tagliaferro, A.R.2    Bobilya, D.J.3
  • 6
    • 0032750323 scopus 로고    scopus 로고
    • Free radical scavenging and antioxidant activities of flavonoids extracted from the radix of scutellaria baicalensis georgi
    • Gao Z, Huang K, Yang X, Xu H: Free radical scavenging and antioxidant activities of flavonoids extracted from the radix of Scutellaria baicalensis Georgi. Biochim Biophys Acta 1472:643–650, 1999.
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 643-650
    • Gao, Z.1    Huang, K.2    Yang, X.3    Xu, H.4
  • 7
    • 0037372798 scopus 로고    scopus 로고
    • Establishment of a quantitative structure-activity relationship model for evaluating and predicting the protective potentials of phenolic antioxidants on lipid peroxidation
    • Cheng Z, Ren J, Li Y, Chang W, Chen Z: Establishment of a quantitative structure-activity relationship model for evaluating and predicting the protective potentials of phenolic antioxidants on lipid peroxidation. J Pharm Sci 92:475–484, 2003.
    • (2003) J Pharm Sci , vol.92 , pp. 475-484
    • Cheng, Z.1    Ren, J.2    Li, Y.3    Chang, W.4    Chen, Z.5
  • 8
    • 0026060983 scopus 로고
    • Inhibitory effects of phenolic compounds on ccl4-induced microsomal lipid peroxidation
    • Cholbi MR, Paya M, Alcaraz MJ: Inhibitory effects of phenolic compounds on CCl4-induced microsomal lipid peroxidation. Experientia 47:195–199, 1991.
    • (1991) Experientia , vol.47 , pp. 195-199
    • Cholbi, M.R.1    Paya, M.2    Alcaraz, M.J.3
  • 9
    • 34547148498 scopus 로고    scopus 로고
    • Ldl isolation and copper-catalysed oxidation
    • Taniguchi N, Gutteridge MC (eds):, New York: Oxford University Press, pp
    • Yokode M, Kita T: LDL isolation and copper-catalysed oxidation. In Taniguchi N, Gutteridge MC (eds): “Experimental Protocols for Reactive Oxygen and Nitrogen Species.” New York: Oxford University Press, pp149–151, 2000.
    • (2000) Experimental Protocols for Reactive Oxygen and Nitrogen Species. , pp. 149-151
    • Yokode, M.1    Kita, T.2
  • 10
    • 0032129206 scopus 로고    scopus 로고
    • Thiol chelation of cu2+ by dihydrolipoic acid prevents human low density lipoprotein peroxidation
    • Lodge JK, Traber MG, Packer L: Thiol chelation of Cu2+ by dihydrolipoic acid prevents human low density lipoprotein peroxidation. Free Radic Biol Med 25:287–297, 1998.
    • (1998) Free Radic Biol Med , vol.25 , pp. 287-297
    • Lodge, J.K.1    Traber, M.G.2    Packer, L.3
  • 11
    • 0031436825 scopus 로고    scopus 로고
    • Influence of green tea and its three major components upon low-density lipoprotein oxidation
    • Yokozawa T, Dong E: Influence of green tea and its three major components upon low-density lipoprotein oxidation. Exp Toxicol Pathol 49:329–335, 1997.
    • (1997) Exp Toxicol Pathol , vol.49 , pp. 329-335
    • Yokozawa, T.1    Dong, E.2
  • 13
    • 85011163770 scopus 로고    scopus 로고
    • Isolation, identification and quantitative determination of gingerols in ginger roots
    • Nazemiyeh H, Delazar A, Afshar J, Eskandari B: Isolation, identification and quantitative determination of gingerols in ginger roots. Ulum-i Daroei 2002(2):61–68, 2002.
    • (2002) Ulum-I Daroei , vol.2002 , Issue.2 , pp. 61-68
    • Nazemiyeh, H.1    Delazar, A.2    Afshar, J.3    Eskandari, B.4
  • 14
    • 85011249723 scopus 로고    scopus 로고
    • Who monographs on selected medicinal plants. Volume i
    • WHO: “WHO monographs on selected medicinal plants. Volume I.” Geneva: World Health Organization, p 37, 1999.
    • (1999) Geneva: World Health Organization , pp. 37
  • 15
    • 0026695202 scopus 로고
    • Role of oxidized low-density lipoprotein in atherogenesis
    • Parthasarathy S, Rankin SM: Role of oxidized low-density lipoprotein in atherogenesis. Prog Lipid Res 31:127–143, 1992.
    • (1992) Prog Lipid Res , vol.31 , pp. 127-143
    • Parthasarathy, S.1    Rankin, S.M.2
  • 17
    • 0030023384 scopus 로고    scopus 로고
    • Hemoglobin induced apoliproprotein b crosslinking in low-density lipoprotein peroxidation
    • Miller YI, Felikman Y, Shaklai N: Hemoglobin induced apoliproprotein B crosslinking in low-density lipoprotein peroxidation. Arch Biochem Biophys 326:252–260, 1996.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 252-260
    • Miller, Y.I.1    Felikman, Y.2    Shaklai, N.3
  • 18
    • 0037794084 scopus 로고    scopus 로고
    • Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron
    • Grinshtein N, Bamm VV, Tsemakhovich VA, Shaklai N: Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron. Biochemistry 42:6977–6985, 2003.
    • (2003) Biochemistry , vol.42 , pp. 6977-6985
    • Grinshtein, N.1    Bamm, V.V.2    Tsemakhovich, V.A.3    Shaklai, N.4
  • 20
    • 0021885797 scopus 로고
    • Reduced levels of plasma ascorbic acid (Vitamin c) in sickle cell disease patients: Its possible role in the oxidant damage to sickle cells in vivo
    • Jain SK, Williams DM: Reduced levels of plasma ascorbic acid (vitamin C) in sickle cell disease patients: its possible role in the oxidant damage to sickle cells in vivo. Clin Chim Acta 149: 257–261, 1985.
    • (1985) Clin Chim Acta , vol.149 , pp. 257-261
    • Jain, S.K.1    Williams, D.M.2
  • 22
    • 0029152979 scopus 로고
    • Mechanism of free radical-induced hemolysis of human erythrocytes: Hemolysis by water-soluble radical initiator
    • Sato Y, Kamo S, Takahashi T, Suzuki Y: Mechanism of free radical-induced hemolysis of human erythrocytes: hemolysis by water-soluble radical initiator. Biochemistry 34:8940–8949, 1995.
    • (1995) Biochemistry , vol.34 , pp. 8940-8949
    • Sato, Y.1    Kamo, S.2    Takahashi, T.3    Suzuki, Y.4
  • 23
    • 0025257164 scopus 로고
    • Ascorbate protects against tert-butyl hydroperoxide inhibition of erythrocyte membrane ca2+, mg2+ atpase
    • Moore RB, Bamberg AD, Wilson LC, Jenkins LD, Mankad VN: Ascorbate protects against tert-butyl hydroperoxide inhibition of erythrocyte membrane Ca2+, Mg2+ ATPase. Arch Biochem Biophys 278:416–424, 1990.
    • (1990) Arch Biochem Biophys , vol.278 , pp. 416-424
    • Moore, R.B.1    Bamberg, A.D.2    Wilson, L.C.3    Jenkins, L.D.4    Mankad, V.N.5
  • 24
    • 0031010544 scopus 로고    scopus 로고
    • Decrease in accessible thiols as an index of oxidative damage to membrane proteins
    • Soszynski M, Bartosz G: Decrease in accessible thiols as an index of oxidative damage to membrane proteins. Free Radic Biol Med 23:463–469, 1997.
    • (1997) Free Radic Biol Med , vol.23 , pp. 463-469
    • Soszynski, M.1    Bartosz, G.2
  • 25
    • 0024203361 scopus 로고
    • Oxidative hemolysis of erythrocytes and its inhibition by free radical scavengers
    • Niki E, Komuro E, Takahashi M, Urano S, Ito E, Terao K: Oxidative hemolysis of erythrocytes and its inhibition by free radical scavengers. J Biol Chem 263:19809–19814, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 19809-19814
    • Niki, E.1    Komuro, E.2    Takahashi, M.3    Urano, S.4    Ito, E.5    Terao, K.6
  • 26
    • 0029938329 scopus 로고    scopus 로고
    • The effects of tert-butyl hydroperoxide on human erythrocyte membrane ion transport and the protective actions of antioxidants
    • Dwight JF, Hendry BM: The effects of tert-butyl hydroperoxide on human erythrocyte membrane ion transport and the protective actions of antioxidants. Clin Chim Acta 249:167–181, 1996.
    • (1996) Clin Chim Acta , vol.249 , pp. 167-181
    • Dwight, J.F.1    Hendry, B.M.2
  • 27
    • 34547219988 scopus 로고    scopus 로고
    • Change of activities of adenosine triphosphatase and superoxide dismutase, erythrocyte na+, k+, ca2+ and mg2+, lipid peroxide in coronary heart disease
    • Zhou X, Lin M, Guo Y: Change of activities of adenosine triphosphatase and superoxide dismutase, erythrocyte Na+, K+, Ca2+ and Mg2+, lipid peroxide in coronary heart disease. Chin J Hypertension 7:24–26, 1999.
    • (1999) Chin J Hypertension , vol.7 , pp. 24-26
    • Zhou, X.1    Lin, M.2    Guo, Y.3
  • 28
    • 0028673872 scopus 로고
    • Measurement of atpase in red cells: Setting up and validation of a highly reproducible method
    • Matteucci E, Cocci F, Pellegrim L, Gregori G., Giampietro O: Measurement of ATPase in red cells: setting up and validation of a highly reproducible method. Enzyme Protein 48:105–119, 1995.
    • (1995) Enzyme Protein , vol.48 , pp. 105-119
    • Matteucci, E.1    Cocci, F.2    Pellegrim, L.3    Gregori, G.4    Giampietro, O.5
  • 29
    • 0028574776 scopus 로고
    • Oxidative crosslinking of ldl protein induced by hemin: Involvement of tyrosines
    • Miller YI, Shaklai N: Oxidative crosslinking of LDL protein induced by hemin: involvement of tyrosines. Biochem Mol Biol Int 34:1121–1129, 1994.
    • (1994) Biochem Mol Biol Int , vol.34 , pp. 1121-1129
    • Miller, Y.I.1    Shaklai, N.2
  • 32
    • 0033837854 scopus 로고    scopus 로고
    • Protective effects of boldine against free radical-induced erythrocyte lysis
    • Jimenez I, Garrido A, Bannach R, Gotteland M, Speisky H: Protective effects of boldine against free radical-induced erythrocyte lysis. Phytother Res 14:339–343, 2000.
    • (2000) Phytother Res , vol.14 , pp. 339-343
    • Jimenez, I.1    Garrido, A.2    Bannach, R.3    Gotteland, M.4    Speisky, H.5
  • 33
    • 0020463375 scopus 로고
    • Standardized method for the determination of human erythrocyte membrane adenosine triphosphatases
    • Reinila M, MacDonald E, Salem N Jr, Linnoila M, Trams EG: Standardized method for the determination of human erythrocyte membrane adenosine triphosphatases. Anal Biochem 124:19–26, 1982.
    • (1982) Anal Biochem , vol.124 , pp. 19-26
    • Reinila, M.1    MacDonald, E.2    Salem, N.3    Linnoila, M.4    Trams, E.G.5
  • 34
    • 0036524623 scopus 로고    scopus 로고
    • Inhibition of atpases by cleistocalyx operculatus. A possible mechanism for the cardiotonic actions of the herb
    • Woo AYH, Waye MMY, Kwan HS, Chan MCY, Chau CF, Cheng CHK: Inhibition of ATPases by Cleistocalyx operculatus. A possible mechanism for the cardiotonic actions of the herb. Vasc Pharmacol 38:163–168, 2002.
    • (2002) Vasc Pharmacol , vol.38 , pp. 163-168
    • Woo, A.1    Waye, M.2    Kwan, H.S.3    Chan, M.4    Chau, C.F.5    Cheng, C.6
  • 35
    • 0018091301 scopus 로고
    • Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane
    • Haest CW, Plasa G, Kamp D, Deuticke B: Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane. Biochim Biophys Acta 509:21–32, 1978.
    • (1978) Biochim Biophys Acta , vol.509 , pp. 21-32
    • Haest, C.W.1    Plasa, G.2    Kamp, D.3    Deuticke, B.4
  • 37
    • 0026778405 scopus 로고
    • Structure revision of 4-hydroxyaloin: 10-hydroxyaloins a and b as main in vitro-oxidation products of the diastereomeric aloins
    • Rauwald HW, Lohse K: Structure revision of 4-hydroxyaloin: 10-Hydroxyaloins A and B as main in vitro-oxidation products of the diastereomeric aloins. Planta Med 58:259–262, 1992.
    • (1992) Planta Med , vol.58 , pp. 259-262
    • Rauwald, H.W.1    Lohse, K.2
  • 38
    • 0023043561 scopus 로고
    • Inhibition of erythrocyte ca2+-atpase by activated oxygen through thiol-and lipiddependent mechanisms
    • Hebbel RP, Shalev O, Foker W, Rank BH: Inhibition of erythrocyte Ca2+-ATPase by activated oxygen through thiol-and lipiddependent mechanisms. Biochim Biophys Acta 862:8–16, 1986.
    • (1986) Biochim Biophys Acta , vol.862 , pp. 8-16
    • Hebbel, R.P.1    Shalev, O.2    Foker, W.3    Rank, B.H.4
  • 39
    • 0029009311 scopus 로고
    • Inhibition of cardiac sarcolemma na+k2+atpase by oxyradical generating systems
    • Shao Q, Matsubara T, Bhatt SK, Dhalla NS: Inhibition of cardiac sarcolemma Na+K2+ATPase by oxyradical generating systems. Mol Cell Biochem 147:139–144, 1995.
    • (1995) Mol Cell Biochem , vol.147 , pp. 139-144
    • Shao, Q.1    Matsubara, T.2    Bhatt, S.K.3    Dhalla, N.S.4
  • 40
    • 0025299187 scopus 로고
    • Radical-induced inactivation of kidney na+, k+-atpase: Sensitivity to membrane lipid peroxidation and the protective effect of vitamin
    • Thomas CE, Reed DJ: Radical-induced inactivation of kidney Na+, K+-ATPase: Sensitivity to membrane lipid peroxidation and the protective effect of vitamin E. Arch Biochem Biophys 281:96–105, 1990.
    • (1990) E. Arch Biochem Biophys , vol.281 , pp. 96-105
    • Thomas, C.E.1    Reed, D.J.2
  • 41
    • 3042849117 scopus 로고    scopus 로고
    • Protective effect of ginger, zingiber officinale rosc on experimental atherosclerosis in rabbits
    • Verma SK, Singh M, Jain P, Bordia A: Protective effect of ginger, Zingiber officinale Rosc on experimental atherosclerosis in rabbits. Indian J Exp Biol 42:736–738, 2004.
    • (2004) Indian J Exp Biol , vol.42 , pp. 736-738
    • Verma, S.K.1    Singh, M.2    Jain, P.3    Bordia, A.4
  • 42
    • 0034011401 scopus 로고    scopus 로고
    • Ginger extract consumption reduces plasma cholesterol, inhibits ldl oxidation and attenuates development of atherosclerosis in atherosclerotic, apolipoprotein e-deficient mice
    • Fuhrman B, Rosenblat M, Hayek T, Coleman R, Aviram M: Ginger extract consumption reduces plasma cholesterol, inhibits LDL oxidation and attenuates development of atherosclerosis in atherosclerotic, apolipoprotein E-deficient mice. J Nutr 130:1124–1131, 2000.
    • (2000) J Nutr , vol.130 , pp. 1124-1131
    • Fuhrman, B.1    Rosenblat, M.2    Hayek, T.3    Coleman, R.4    Aviram, M.5
  • 43
    • 0041571830 scopus 로고    scopus 로고
    • Effect of zingiber officinale rosc on lipid peroxidation in hyperlipidemia rats
    • Liu N, Huo G, Zhang L, Zhang X: Effect of Zingiber officinale Rosc on lipid peroxidation in hyperlipidemia rats. Wei Sheng Yan Jiu 32:22–23, 2003.
    • (2003) Wei Sheng Yan Jiu , vol.32 , pp. 22-23
    • Liu, N.1    Huo, G.2    Zhang, L.3    Zhang, X.4
  • 44
    • 12344264705 scopus 로고    scopus 로고
    • Modulatory effects of aloe vera leaf gel extract on oxidative stress in rats treated with streptozotocin
    • Rajasekaran S, Sivagnanam K, Subramanian S: Modulatory effects of Aloe vera leaf gel extract on oxidative stress in rats treated with streptozotocin. J Pharm Pharmacol 57:241–246, 2005.
    • (2005) J Pharm Pharmacol , vol.57 , pp. 241-246
    • Rajasekaran, S.1    Sivagnanam, K.2    Subramanian, S.3
  • 45
    • 18044363640 scopus 로고    scopus 로고
    • Antioxidant effect of aloe vera leaf gel extract in streptozotocin-induced diabetes in rats
    • Rajasekaran S, Sivagnanam K, Subramanian S: Antioxidant effect of Aloe vera leaf gel extract in streptozotocin-induced diabetes in rats. Pharmacol Rep 57:90–96, 2005.
    • (2005) Pharmacol Rep , vol.57 , pp. 90-96
    • Rajasekaran, S.1    Sivagnanam, K.2    Subramanian, S.3
  • 46
    • 2342512006 scopus 로고    scopus 로고
    • Susceptibility of hippocampus and cerebral cortex to oxidative damage in streptozotocin treated mice: Prevention by extracts of withania somnifera and aloe vera
    • Parihar MS, Chaudhary M, Shetty R, Hemnani T: Susceptibility of hippocampus and cerebral cortex to oxidative damage in streptozotocin treated mice: prevention by extracts of Withania somnifera and Aloe vera. J Clin Neurosci 11:397–402, 2004.
    • (2004) J Clin Neurosci , vol.11 , pp. 397-402
    • Parihar, M.S.1    Chaudhary, M.2    Shetty, R.3    Hemnani, T.4
  • 47
    • 0037332298 scopus 로고    scopus 로고
    • Phenolic antioxidants attenuate hippocampal neuronal cell damage against kainic acid induced excitotoxicity
    • Parihar MS, Hemnani T: Phenolic antioxidants attenuate hippocampal neuronal cell damage against kainic acid induced excitotoxicity. J Biosci 28:121–128, 2003.
    • (2003) J Biosci , vol.28 , pp. 121-128
    • Parihar, M.S.1    Hemnani, T.2
  • 48
    • 0346366651 scopus 로고    scopus 로고
    • Effectiveness of aloe vera on the antioxidant status of different tissues in irradiated rats
    • Saada HN, Ussama ZS, Mahdy AM: Effectiveness of Aloe vera on the antioxidant status of different tissues in irradiated rats. Pharmazie 58:929–931, 2003.
    • (2003) Pharmazie , vol.58 , pp. 929-931
    • Saada, H.N.1    Ussama, Z.S.2    Mahdy, A.M.3
  • 49
    • 0034044657 scopus 로고    scopus 로고
    • Chemomodulatory action of aloe vera on the profiles of enzymes associated with carcinogen metabolism and antioxidant status regulation in mice
    • Singh RP, Dhanalakshmi S, Rao AR: Chemomodulatory action of Aloe vera on the profiles of enzymes associated with carcinogen metabolism and antioxidant status regulation in mice. Phytomedicine 7:209–219, 2000.
    • (2000) Phytomedicine , vol.7 , pp. 209-219
    • Singh, R.P.1    Dhanalakshmi, S.2    Rao, A.R.3
  • 51
    • 84893483639 scopus 로고
    • Antioxidant effects of some ginger constituents
    • Kikuzaki H, Nakayani N: Antioxidant effects of some ginger constituents. J Food Sci 58:1407–1410, 1993.
    • (1993) J Food Sci , vol.58 , pp. 1407-1410
    • Kikuzaki, H.1    Nakayani, N.2
  • 53
  • 54
    • 0033921138 scopus 로고    scopus 로고
    • Antioxidant activity of anthraquinones and anthrone
    • Yen GC, Duh PD, Chuang DY: Antioxidant activity of anthraquinones and anthrone. Food Chem 70:437–441, 2000.
    • (2000) Food Chem , vol.70 , pp. 437-441
    • Yen, G.C.1    Duh, P.D.2    Chuang, D.Y.3
  • 55
    • 0030824909 scopus 로고    scopus 로고
    • Antioxidant actions of anthraquinolines contained in rheum
    • Yuan Z, Gao R: Antioxidant actions of anthraquinolines contained in Rheum. Pharm Pharmacol Lett 7:9–12, 1997.
    • (1997) Pharm Pharmacol Lett , vol.7 , pp. 9-12
    • Yuan, Z.1    Gao, R.2
  • 56
    • 0035190362 scopus 로고    scopus 로고
    • Antioxidant constituents from rhubarb: Structural requirements of stilbenes for the activity and structures of two new anthraquinone glucosides
    • Matsuda H, Morikawa T, Toguchida I, Park JY, Harima S, Yoshikawa M: Antioxidant constituents from rhubarb: structural requirements of stilbenes for the activity and structures of two new anthraquinone glucosides. Bioorg Med Chem 9:41–50, 2001.
    • (2001) Bioorg Med Chem , vol.9 , pp. 41-50
    • Matsuda, H.1    Morikawa, T.2    Toguchida, I.3    Park, J.Y.4    Harima, S.5    Yoshikawa, M.6
  • 57
    • 85011153287 scopus 로고
    • Biochemical study of chinese rhubarb. Xxiv. Inhibitory effects of anthraquinonen derivatives on some flavinlinked enzymes
    • He BF, Chen QH: Biochemical study of Chinese rhubarb. XXIV. Inhibitory effects of anthraquinonen derivatives on some flavinlinked enzymes. Acta Biochim Biophys Sin 21:72–77, 1989.
    • (1989) Acta Biochim Biophys Sin , vol.21 , pp. 72-77
    • He, B.F.1    Chen, Q.H.2


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