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Volumn 154, Issue 3, 1999, Pages 287-291

Arsenite methylation by methylvitamin B12 and glutathione does not require an enzyme

Author keywords

Arsenic biotransformation; DMPS; GSH; Methylcobalamin; Methylvitamin B12; MMA; Selenium

Indexed keywords

ARSENIC TRIOXIDE; GLUTATHIONE; MECOBALAMIN;

EID: 0033012169     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1006/taap.1998.8587     Document Type: Article
Times cited : (62)

References (32)
  • 1
    • 0008517022 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic species and other new approaches to arsenic toxicity
    • Aposhian H. V. Enzymatic methylation of arsenic species and other new approaches to arsenic toxicity. Annu. Rev. Pharmacol. Toxicol. 37:1997;397-419.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 397-419
    • Aposhian, H.V.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation 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
  • 3
    • 0021866517 scopus 로고
    • Study of inorganic arsenic methylation by rat liverin vitro:
    • Buchet J. P., Lauwerys R. Study of inorganic arsenic methylation by rat liverin vitro: Arch. Toxicol. 57:1985;125-129.
    • (1985) Arch. Toxicol. , vol.57 , pp. 125-129
    • Buchet, J.P.1    Lauwerys, R.2
  • 5
    • 84889770800 scopus 로고
    • Biological methylation
    • Challenger F. Biological methylation. Adv. Enzymol. 12:1951;429-491.
    • (1951) Adv. Enzymol. , vol.12 , pp. 429-491
    • Challenger, F.1
  • 7
    • 33845184777 scopus 로고
    • Arsenic speciation in the environment
    • Cullen W. R., Reimer K. J. Arsenic speciation in the environment. Chem. Rev. 89:1989;713-764.
    • (1989) Chem. Rev. , vol.89 , pp. 713-764
    • Cullen, W.R.1    Reimer, K.J.2
  • 8
    • 85030355215 scopus 로고
    • Kinetics of ingested radiocyanocobalamin
    • Stuttgart: Verlag. p. 381-396
    • 12. 1962;Verlag, Stuttgart. p. 381-396.
    • (1962) 12
    • Dorscherholmen, A.1    Hagen, P.S.2
  • 9
    • 85030355964 scopus 로고
    • 12
    • R. Ammon, & G. T. Dirschirl. Stuttgart: Verlag
    • 12. Ammon R., Dirschirl G. T. Fermente-Hormone-Vitamine. 1975;319-327 Verlag, Stuttgart.
    • (1975) Fermente-Hormone-Vitamine , pp. 319-327
    • Friedrich, W.1
  • 10
    • 84989547977 scopus 로고
    • The ion-chromatography behavior of arsenite, arsenate, methylarsonic acid and dimethylarsinic acid on the Hamilton PRP-X100 anion exchange column
    • Gailer J., Irgolic K. J. The ion-chromatography behavior of arsenite, arsenate, methylarsonic acid and dimethylarsinic acid on the Hamilton PRP-X100 anion exchange column. Appl. Organomet. Chem. 8:1994;129-140.
    • (1994) Appl. Organomet. Chem. , vol.8 , pp. 129-140
    • Gailer, J.1    Irgolic, K.J.2
  • 11
    • 85030354045 scopus 로고
    • 1212
    • G. Litwack. New York: Academic Press
    • 1212. Litwack G. Vitamins and Hormones. 1995;1-76 Academic Press, New York.
    • (1995) Vitamins and Hormones , pp. 1-76
    • Glusker, J.P.1
  • 15
    • 0030793517 scopus 로고    scopus 로고
    • Healy, S. M. Zakharyan, R. A. Aposhian, H. V. 1997, Enzymatic methylation of arsenic compounds: IV.In vitroin vivo, Mutat. Res. 386, 229, 239, Mutat. Res. 387, 173.
    • Mutat. Res. , vol.387 , pp. 173
  • 17
    • 0022388672 scopus 로고
    • Methyl transfer from methylcobalamin to thiols. A reinvestigation
    • Hogenkamp H. P., Bratt G. T., Sun S.-Z. Methyl transfer from methylcobalamin to thiols. A reinvestigation. Biochemistry. 24:1985;6428-6432.
    • (1985) Biochemistry , vol.24 , pp. 6428-6432
    • Hogenkamp, H.P.1    Bratt, G.T.2    Sun, S.-Z.3
  • 18
    • 0006052339 scopus 로고
    • The fate of cobalaminin vivo.
    • B. M. Babior. New York: John Willey and Sons
    • Linnel T. C. The fate of cobalaminin vivo. Babior B. M. Cobalamin: Biochemistry and Pathology. 1974;288-333 John Willey and Sons, New York.
    • (1974) Cobalamin: Biochemistry and Pathology , pp. 288-333
    • Linnel, T.C.1
  • 19
    • 0015146401 scopus 로고
    • Biosynthesis of dimethylarsine by methanobacterium
    • McBride B. C., Wolfe R. S. Biosynthesis of dimethylarsine by methanobacterium. Biochemistry. 10:1971;4312-4317.
    • (1971) Biochemistry , vol.10 , pp. 4312-4317
    • McBride, B.C.1    Wolfe, R.S.2
  • 21
    • 0025290614 scopus 로고
    • Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes
    • Pezacka E., Green R., Jacobsen D. W. Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem. Biophys. Res. Commun. 169:1990;443-450.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 443-450
    • Pezacka, E.1    Green, R.2    Jacobsen, D.W.3
  • 22
    • 0344249077 scopus 로고
    • Biosynthesis of methylcobalamin: Chemical model studies with thiol-cobalamin adducts and adenosylmethionine
    • Pezacka E. H., Denison C. J., Green R., Jacobsen D. W. Biosynthesis of methylcobalamin: Chemical model studies with thiol-cobalamin adducts and adenosylmethionine. J. Cell Biol. 107:1988.
    • (1988) J. Cell Biol. , vol.107
    • Pezacka, E.H.1    Denison, C.J.2    Green, R.3    Jacobsen, D.W.4
  • 24
    • 0015858134 scopus 로고
    • Reductive dealkylation of alkylcobaloximes, alkylcobalamins, and related compounds. Simulation of corrin dependent reductase and methylgroup transfer reactions
    • Schrauzer G. N., Seck J., Holland R., Beckhan T., Rubin E., Sibert J. Reductive dealkylation of alkylcobaloximes, alkylcobalamins, and related compounds. Simulation of corrin dependent reductase and methylgroup transfer reactions. Bioinorg. Chem. 2:1973;93-124.
    • (1973) Bioinorg. Chem. , vol.2 , pp. 93-124
    • Schrauzer, G.N.1    Seck, J.2    Holland, R.3    Beckhan, T.4    Rubin, E.5    Sibert, J.6
  • 25
    • 0030034424 scopus 로고    scopus 로고
    • Mono- And dimethylation of arsenic in rat liver cytosol in vitro
    • Styblo M., Delnomdedieu M., Thomas D. J. Mono- and dimethylation of arsenic in rat liver cytosol in vitro. Chem.-Biol. Interact. 99:1996;147-164.
    • (1996) Chem.-Biol. Interact. , vol.99 , pp. 147-164
    • Styblo, M.1    Delnomdedieu, M.2    Thomas, D.J.3
  • 28
    • 0023357951 scopus 로고
    • Effects of low dietary intake of methionine, choline or proteins on the biotransformation of arsenite in the rabbit
    • Vahter M., Marafante E. Effects of low dietary intake of methionine, choline or proteins on the biotransformation of arsenite in the rabbit. Toxicol. Lett. 37:1987;41-46.
    • (1987) Toxicol. Lett. , vol.37 , pp. 41-46
    • Vahter, M.1    Marafante, E.2
  • 29
    • 0032192180 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic compounds: VI. Characterization of hamster liver arsenite and methylarsonic acid methyltransferase activitiesin vitro
    • Wildfang E., Zakharyan R. A., Aposhian H. V. Enzymatic methylation of arsenic compounds: VI. Characterization of hamster liver arsenite and methylarsonic acid methyltransferase activitiesin vitro. Toxicol. Appl. Pharmacol. 152:1998;366-375.
    • (1998) Toxicol. Appl. Pharmacol. , vol.152 , pp. 366-375
    • Wildfang, E.1    Zakharyan, R.A.2    Aposhian, H.V.3
  • 30
    • 0013364544 scopus 로고
    • 12
    • B. Zagalak, & W. Friedrich. Berlin, New York: Walter de Gruyter
    • 12. 1979;539-556 Walter de Gruyter, Berlin, New York.
    • (1979) 12 , pp. 539-556
    • Wood, J.M.1    Fanchiang, Y.T.2
  • 31
    • 0030247067 scopus 로고    scopus 로고
    • Enzymatic methylation of arsenic compounds: III. The marmoset and tamarin, but not the rhesus, monkey are deficient in methyltransferases that methylate inorganic arsenic
    • Zakharyan R. A., Wildfang E., Aposhian H. V. Enzymatic methylation of arsenic compounds: III. The marmoset and tamarin, but not the rhesus, monkey are deficient in methyltransferases that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140:1996;77-84.
    • (1996) Toxicol. Appl. Pharmacol. , vol.140 , pp. 77-84
    • Zakharyan, R.A.1    Wildfang, E.2    Aposhian, H.V.3
  • 32
    • 0028861888 scopus 로고
    • Enzymatic methylation of arsenic compounds. I: Assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver
    • Zakharyan R., Wu Y., Bogdan G. M., Aposhian H. V. Enzymatic methylation of arsenic compounds. I: Assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. Chem. Res. Toxicol. 8:1995;1029-1038.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 1029-1038
    • Zakharyan, R.1    Wu, Y.2    Bogdan, G.M.3    Aposhian, H.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.