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Volumn 97, Issue 1-2, 1998, Pages 33-44

Molecular cloning and characterization of the genes encoding two isoforms of cysteine synthase in the enteric protozoan parasite Entamoeba histolytica1

Author keywords

Anti oxidant; Cysteine; Cysteine synthase; Entamoeba histolytica

Indexed keywords

CYSTEINE; CYSTEINE SYNTHASE;

EID: 0032583190     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00129-7     Document Type: Article
Times cited : (86)

References (54)
  • 1
    • 0003478367 scopus 로고
    • Report of the Director-General. Geneva: World Health Organization
    • World Health Organization. The World Health Report 1995: Bridging the Gaps; Report of the Director-General. Geneva: World Health Organization, 1995.
    • (1995) The World Health Report 1995: Bridging the Gaps
  • 2
    • 0016382328 scopus 로고
    • Entamoeba histolytica I aerobic metabolism
    • Weinbach E.C., Diamond L. Entamoeba histolytica I aerobic metabolism. Exp Parasitol. 35:1974;232-243.
    • (1974) Exp Parasitol , vol.35 , pp. 232-243
    • Weinbach, E.C.1    Diamond, L.2
  • 3
    • 0030458544 scopus 로고    scopus 로고
    • Antioxidant defense mechanisms in parasitic protozoa
    • Mehlotra R. Antioxidant defense mechanisms in parasitic protozoa. Crit Rev Microbiol. 22:1996;295-314.
    • (1996) Crit Rev Microbiol , vol.22 , pp. 295-314
    • Mehlotra, R.1
  • 4
    • 0026316667 scopus 로고
    • Molecular and cellular characterization of the 29-kilodalton peripheral membrane protein of Entamoeba histolytica: Differentiation between pathogenic and nonpathogenic isolates
    • Reed S.L., Flores B.M., Batzer M.A. et al. Molecular and cellular characterization of the 29-kilodalton peripheral membrane protein of Entamoeba histolytica: differentiation between pathogenic and nonpathogenic isolates. Infect Immun. 60:1992;542-549.
    • (1992) Infect Immun , vol.60 , pp. 542-549
    • Reed, S.L.1    Flores, B.M.2    Batzer, M.A.3
  • 5
    • 0027196296 scopus 로고
    • Analysis of the genomic sequence encoding the 29 kDa cysteine-rich protein of Entamoeba histolytica
    • Bruchhaus I., Tannich E. Analysis of the genomic sequence encoding the 29 kDa cysteine-rich protein of Entamoeba histolytica. Trop Med Parasitol. 44:1993;116-118.
    • (1993) Trop Med Parasitol , vol.44 , pp. 116-118
    • Bruchhaus, I.1    Tannich, E.2
  • 6
    • 0028914574 scopus 로고
    • Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases
    • Bruchhaus I., Tannich E. Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases. Mol Biochem Parasitol. 70:1995;187-191.
    • (1995) Mol Biochem Parasitol , vol.70 , pp. 187-191
    • Bruchhaus, I.1    Tannich, E.2
  • 8
    • 0019830957 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Effects of cysteine and oxygen tension on trophozoite attachment to glass and survival in culture media
    • Gillin F.D., Diamond L.S. Entamoeba histolytica and Giardia lamblia: effects of cysteine and oxygen tension on trophozoite attachment to glass and survival in culture media. Exp Parasitol. 52:1981;9-17.
    • (1981) Exp Parasitol , vol.52 , pp. 9-17
    • Gillin, F.D.1    Diamond, L.S.2
  • 9
    • 0019253877 scopus 로고
    • Attachment of Entamoeba histolytica to glass in a defined maintenance medium: Specific requirement for cysteine and ascorbic acid
    • Gillin F.D., Diamond L.S. Attachment of Entamoeba histolytica to glass in a defined maintenance medium: specific requirement for cysteine and ascorbic acid. J Protozool. 27:1980;474-478.
    • (1980) J Protozool , vol.27 , pp. 474-478
    • Gillin, F.D.1    Diamond, L.S.2
  • 10
    • 0024040340 scopus 로고
    • DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH
    • Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M. DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH. J Bacteriol. 170:1988;3150-3157.
    • (1988) J Bacteriol , vol.170 , pp. 3150-3157
    • Byrne, C.R.1    Monroe, R.S.2    Ward, K.A.3    Kredich, N.M.4
  • 11
    • 0028700721 scopus 로고
    • Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
    • Ogasawara N., Nakai S., Yoshikawa H. Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin. DNA Res. 1:1994;1-14.
    • (1994) DNA Res , vol.1 , pp. 1-14
    • Ogasawara, N.1    Nakai, S.2    Yoshikawa, H.3
  • 12
    • 0028025227 scopus 로고
    • Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
    • Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R. Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana. FEBS Lett. 351:1994;257-262.
    • (1994) FEBS Lett , vol.351 , pp. 257-262
    • Hell, R.1    Bork, C.2    Bogdanova, N.3    Frolov, I.4    Hauschild, R.5
  • 13
    • 0028229630 scopus 로고
    • Molecular cloning of a cysteine synthase cDNA from Citrullus vulgaris (watermelon) by genetic complementation in an Escherichia coli Cys-auxotroph
    • Noji M., Murakoshi I., Saito K. Molecular cloning of a cysteine synthase cDNA from Citrullus vulgaris (watermelon) by genetic complementation in an Escherichia coli Cys-auxotroph. Mol Gen Genet. 244:1994;57-66.
    • (1994) Mol Gen Genet , vol.244 , pp. 57-66
    • Noji, M.1    Murakoshi, I.2    Saito, K.3
  • 14
    • 0026699665 scopus 로고
    • Cysteine synthase from Capsicum annuum chromoplasts. Characterization and cDNA cloning of an up-regulated enzyme during fruit development
    • Romer S., d'Harlingue A., Camara B., Schantz R., Kuntz M. Cysteine synthase from Capsicum annuum chromoplasts. Characterization and cDNA cloning of an up-regulated enzyme during fruit development. J Biol Chem. 267:1992;17966-17970.
    • (1992) J Biol Chem , vol.267 , pp. 17966-17970
    • Romer, S.1    D'Harlingue, A.2    Camara, B.3    Schantz, R.4    Kuntz, M.5
  • 15
    • 0026770274 scopus 로고
    • Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase
    • Saito K., Miura N., Yamazaki M., Hirano H., Murakoshi I. Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase. Proc Natl Acad Sci USA. 89:1992;8078-8082.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8078-8082
    • Saito, K.1    Miura, N.2    Yamazaki, M.3    Hirano, H.4    Murakoshi, I.5
  • 16
    • 0027288172 scopus 로고
    • CDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea
    • Saito K., Tatsuguchi K., Murakoshi I., Hirano H. cDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea. FEBS Lett. 324:1993;247-252.
    • (1993) FEBS Lett , vol.324 , pp. 247-252
    • Saito, K.1    Tatsuguchi, K.2    Murakoshi, I.3    Hirano, H.4
  • 17
    • 0028097282 scopus 로고
    • Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol)-lyase) from Spinacia oleracea
    • Saito K., Tatsuguchi K., Takagi Y., Murakoshi I. Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol)-lyase) from Spinacia oleracea. J Biol Chem. 269:1994;28187-28192.
    • (1994) J Biol Chem , vol.269 , pp. 28187-28192
    • Saito, K.1    Tatsuguchi, K.2    Takagi, Y.3    Murakoshi, I.4
  • 18
    • 0017047142 scopus 로고
    • Subcellular localization of O-acetylserine sulfhydrylase in spinach leaves
    • Fankhauser H., Brunold C., Erismann K.H. Subcellular localization of O-acetylserine sulfhydrylase in spinach leaves. Experientia. 32:1976;1494-1497.
    • (1976) Experientia , vol.32 , pp. 1494-1497
    • Fankhauser, H.1    Brunold, C.2    Erismann, K.H.3
  • 19
    • 0028133985 scopus 로고
    • Enzymic synthesis of non-protein beta-substituted alanines and some higher homologues in plants
    • Ikegami F., Murakoshi I. Enzymic synthesis of non-protein beta-substituted alanines and some higher homologues in plants. Phytochemistry. 35:1994;1089-1104.
    • (1994) Phytochemistry , vol.35 , pp. 1089-1104
    • Ikegami, F.1    Murakoshi, I.2
  • 20
    • 0014890542 scopus 로고
    • Advances in methods of Entamoeba histolytica culture
    • Landa L., Sepulveda B., De la Torre M. Advances in methods of Entamoeba histolytica culture. Arch Invest Med. 1:1970;9-14.
    • (1970) Arch Invest Med , vol.1 , pp. 9-14
    • Landa, L.1    Sepulveda, B.2    De la Torre, M.3
  • 21
    • 0015296466 scopus 로고
    • Viruses of Entamoeba histolytica. I. Identification of transmissible virus-like agents
    • Diamond L.S., Mattern C.F., Bartgis I.L. Viruses of Entamoeba histolytica. I. Identification of transmissible virus-like agents. J Virol. 9:1972;326-341.
    • (1972) J Virol , vol.9 , pp. 326-341
    • Diamond, L.S.1    Mattern, C.F.2    Bartgis, I.L.3
  • 22
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond L.S., Harlow D.R., Cunnick C.C. A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Trans R Soc Trop Med Hyg. 72:1978;431-432.
    • (1978) Trans R Soc Trop Med Hyg , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 23
    • 0010367338 scopus 로고
    • Purification and properties of cysteine synthase from Spinacia oleracea
    • Murakoshi I., Ikegami F., Kaneko M. Purification and properties of cysteine synthase from Spinacia oleracea. Phytochemistry. 24:1985;1907-1911.
    • (1985) Phytochemistry , vol.24 , pp. 1907-1911
    • Murakoshi, I.1    Ikegami, F.2    Kaneko, M.3
  • 24
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitondem M.K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J. 104:1967;627-633.
    • (1967) Biochem J , vol.104 , pp. 627-633
    • Gaitondem, M.K.1
  • 25
    • 44049111777 scopus 로고
    • Purification and characterization of two forms of cysteine synthase from Allium tuberosum
    • Ikegami F., Itagaki S., Murakoshi I. Purification and characterization of two forms of cysteine synthase from Allium tuberosum. Phytochemistry. 32:1993;31-34.
    • (1993) Phytochemistry , vol.32 , pp. 31-34
    • Ikegami, F.1    Itagaki, S.2    Murakoshi, I.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitaion of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitaion of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72:1976;248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0030602236 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein
    • Nozaki T., Haynes P.A., Cross G.A. Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein. Mol Biochem Parasitol. 82:1996;245-255.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 245-255
    • Nozaki, T.1    Haynes, P.A.2    Cross, G.A.3
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 4:1987;406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 33
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J. Confidence limits on phylogenies: an approach using the bootstrap. Evolution. 39:1985;783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 34
    • 0017754041 scopus 로고
    • Isolation and characterization of cysK mutants of Escherichia coli K12
    • Fimmel A.L., Loughlin R.E. Isolation and characterization of cysK mutants of Escherichia coli K12. J Gen Microbiol. 103:1977;37-43.
    • (1977) J Gen Microbiol , vol.103 , pp. 37-43
    • Fimmel, A.L.1    Loughlin, R.E.2
  • 35
    • 0017358849 scopus 로고
    • Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase
    • Burnell J.N., Whatley F.R. Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase. Biochim Biophys Acta. 481:1977;246-265.
    • (1977) Biochim Biophys Acta , vol.481 , pp. 246-265
    • Burnell, J.N.1    Whatley, F.R.2
  • 36
    • 0001575175 scopus 로고
    • Purification and characterization of cysteine synthases from Citrullus vulgaris
    • Ikegami F., Kaneko M., Kamiyama H., Murakoshi F. Purification and characterization of cysteine synthases from Citrullus vulgaris. Phytochemistry. 27:1988;697-701.
    • (1988) Phytochemistry , vol.27 , pp. 697-701
    • Ikegami, F.1    Kaneko, M.2    Kamiyama, H.3    Murakoshi, F.4
  • 37
    • 0023072914 scopus 로고
    • O-acetylserine sulfhydrylase from Bacillus sphaericus
    • Nagasawa T., Yamada H. O-acetylserine sulfhydrylase from Bacillus sphaericus. Methods Enzymol. 143:1987;474-478.
    • (1987) Methods Enzymol , vol.143 , pp. 474-478
    • Nagasawa, T.1    Yamada, H.2
  • 38
    • 0020772846 scopus 로고
    • O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue
    • Hensel G., Truper H.G. O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue. Arch Microbiol. 134:1983;227-232.
    • (1983) Arch Microbiol , vol.134 , pp. 227-232
    • Hensel, G.1    Truper, H.G.2
  • 39
    • 0026447531 scopus 로고
    • Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica
    • Kumar A., Shen P.S., Descoteaux S., Pohl J., Bailey G., Samuelson J. Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica. Proc Natl Acad Sci USA. 89:1992;10188-10192.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10188-10192
    • Kumar, A.1    Shen, P.S.2    Descoteaux, S.3    Pohl, J.4    Bailey, G.5    Samuelson, J.6
  • 40
    • 0027254780 scopus 로고
    • Determination of a functional lysine residue of a plant cysteine synthase by site-directed mutagenesis, and the molecular evolutionary implications
    • Saito K., Kurosawa M., Murakoshi I. Determination of a functional lysine residue of a plant cysteine synthase by site-directed mutagenesis, and the molecular evolutionary implications. FEBS Lett. 328:1993;111-114.
    • (1993) FEBS Lett , vol.328 , pp. 111-114
    • Saito, K.1    Kurosawa, M.2    Murakoshi, I.3
  • 41
    • 0022560056 scopus 로고
    • Molecular biology of DNA in Acanthamoeba, Amoeba, Entamoeba, and Naegleria
    • Byers T.J. Molecular biology of DNA in Acanthamoeba, Amoeba, Entamoeba, and Naegleria. Int Rev Cytol. 99:1986;311-341.
    • (1986) Int Rev Cytol , vol.99 , pp. 311-341
    • Byers, T.J.1
  • 42
    • 0029372798 scopus 로고
    • Elucidation of the DNA synthetic cycle of Entamoeba spp. using flow cytometry and mathematical modeling
    • Dvorak J.A., Kobayashi S., Alling D.W., Hallahan C.W. Elucidation of the DNA synthetic cycle of Entamoeba spp. using flow cytometry and mathematical modeling. J Eukaryot Microbiol. 42:1995;610-616.
    • (1995) J Eukaryot Microbiol , vol.42 , pp. 610-616
    • Dvorak, J.A.1    Kobayashi, S.2    Alling, D.W.3    Hallahan, C.W.4
  • 43
    • 0029068423 scopus 로고
    • Direct evidence for secondary loss of mitochondria in Entamoeba histolytica
    • Clark C.G., Roger A.J. Direct evidence for secondary loss of mitochondria in Entamoeba histolytica. Proc Natl Acad Sci USA. 92:1995;6518-6521.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6518-6521
    • Clark, C.G.1    Roger, A.J.2
  • 44
    • 0027565033 scopus 로고
    • Relative efficiencies of the maximum likelihood, maximum parsimony, and neighbor-joining methods for estimating protein phylogeny
    • Hasegawa M., Fujiwara M. Relative efficiencies of the maximum likelihood, maximum parsimony, and neighbor-joining methods for estimating protein phylogeny. Mol Phylogen Evol. 2:1993;1-5.
    • (1993) Mol Phylogen Evol , vol.2 , pp. 1-5
    • Hasegawa, M.1    Fujiwara, M.2
  • 45
    • 0028362880 scopus 로고
    • Application and accuracy of molecular phylogenies
    • Hillis D.M., Huelsenbeck J.P., Cunningham C.W. Application and accuracy of molecular phylogenies. Science. 264:1994;671-677.
    • (1994) Science , vol.264 , pp. 671-677
    • Hillis, D.M.1    Huelsenbeck, J.P.2    Cunningham, C.W.3
  • 46
    • 0028153888 scopus 로고
    • Protein phylogeny gives a robust estimation for early divergences of eukaryotes: Phylogenetic place of a mitochondria-lacking protozoan; Giardia lamblia
    • Hashimoto T., Nakamura Y., Nakamura F. et al. Protein phylogeny gives a robust estimation for early divergences of eukaryotes: phylogenetic place of a mitochondria-lacking protozoan; Giardia lamblia. Mol Biol Evol. 11:1994;65-71.
    • (1994) Mol Biol Evol , vol.11 , pp. 65-71
    • Hashimoto, T.1    Nakamura, Y.2    Nakamura, F.3
  • 47
    • 0028384696 scopus 로고
    • The uptake and metabolism of cysteine by Giardia lamblia trophozoites
    • Lujan H.D., Nash T.E. The uptake and metabolism of cysteine by Giardia lamblia trophozoites. J Eukaryot Microbiol. 41:1994;169-175.
    • (1994) J Eukaryot Microbiol , vol.41 , pp. 169-175
    • Lujan, H.D.1    Nash, T.E.2
  • 48
    • 0019464089 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Growth responses to reducing agents
    • Gillin F.D., Diamond L.S. Entamoeba histolytica and Giardia lamblia: growth responses to reducing agents. Exp Parasitol. 51:1981;382-391.
    • (1981) Exp Parasitol , vol.51 , pp. 382-391
    • Gillin, F.D.1    Diamond, L.S.2
  • 49
    • 0018745110 scopus 로고
    • Growth response of axenic Entamoeba histolytica to hydrogen, carbon dioxide, and oxygen
    • Band R.N., Cirrito H. Growth response of axenic Entamoeba histolytica to hydrogen, carbon dioxide, and oxygen. J Protozool. 26:1979;282-286.
    • (1979) J Protozool , vol.26 , pp. 282-286
    • Band, R.N.1    Cirrito, H.2
  • 50
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb A.H., Blackburn P., Ulrich P., Chait B.T., Cerami A. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science. 227:1985;1485-1487.
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 51
    • 0031031797 scopus 로고    scopus 로고
    • Isolation and purification of glutathionyl-spermidine and trypanothione from Entamoeba histolytica
    • Ondarza R.N., Tamayo E.M., Hurtado G., Hernandez E., Iturbe A. Isolation and purification of glutathionyl-spermidine and trypanothione from Entamoeba histolytica. Arch Med Res. 28:1997;S73-S75.
    • (1997) Arch Med Res , vol.28
    • Ondarza, R.N.1    Tamayo, E.M.2    Hurtado, G.3    Hernandez, E.4    Iturbe, A.5
  • 52
    • 0025951254 scopus 로고
    • Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction
    • Tachibana H., Ihara S., Kobayashi S., Kaneda Y., Takeuchi T., Watanabe Y. Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction. J Clin Microbiol. 29:1991;2234-2239.
    • (1991) J Clin Microbiol , vol.29 , pp. 2234-2239
    • Tachibana, H.1    Ihara, S.2    Kobayashi, S.3    Kaneda, Y.4    Takeuchi, T.5    Watanabe, Y.6
  • 53
    • 0030778936 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica
    • Bruchhaus I., Richter S., Tannich E. Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica. Biochem J. 326:1997;785-789.
    • (1997) Biochem J , vol.326 , pp. 785-789
    • Bruchhaus, I.1    Richter, S.2    Tannich, E.3
  • 54
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage; Purification and properties
    • Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage; purification and properties. J Biol Chem. 264:1989;1488-1496.
    • (1989) J Biol Chem , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4


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