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Volumn 16, Issue 1, 1996, Pages 77-83

Methylmercury-cysteine uptake by rat erythrocytes: Evidence for several transport systems

Author keywords

Cysteine; Erythrocytes; Lower temperature; Methylmercury; Rats; Transport systems; Uptake

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; CALCIUM; COLCHICINE; CYSTEINE; CYTOCHALASIN B; FLUORIDE SODIUM; GLUCOSE; HEXANOL; HOMOCYSTEINE; METHYLMERCURY; N ETHYLMALEIMIDE; OUABAIN; PROBENECID; VINBLASTINE;

EID: 0030044590     PISSN: 0260437X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1263(199601)16:1<77::AID-JAT319>3.0.CO;2-C     Document Type: Review
Times cited : (22)

References (55)
  • 1
    • 0022551473 scopus 로고
    • Metabolic activation and detoxication of nephrotoxic cysteine and homocysteine S-conjugates
    • A. A. Elfarra, L. H. Lash and W. M. Anders, Metabolic activation and detoxication of nephrotoxic cysteine and homocysteine S-conjugates. Proc. Natl. Acad. Sci. USA 83, 2667-2671 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2667-2671
    • Elfarra, A.A.1    Lash, L.H.2    Anders, W.M.3
  • 2
    • 0021867892 scopus 로고
    • Structure/activity studies of the nephrotoxic and mutagenic action of cysteine conjugates of chloro- And fluoroalkenes
    • T. Green and J. Oddum, Structure/activity studies of the nephrotoxic and mutagenic action of cysteine conjugates of chloro- and fluoroalkenes. Chem. Biol. Interact. 54, 15-31 (1985).
    • (1985) Chem. Biol. Interact. , vol.54 , pp. 15-31
    • Green, T.1    Oddum, J.2
  • 3
    • 0023761451 scopus 로고
    • Studies on the mechanism of nephrotoxicity and nephrocarcinogenicity of halogenated alkenes
    • E. A. Lock, Studies on the mechanism of nephrotoxicity and nephrocarcinogenicity of halogenated alkenes. CRC Crit. Rev. Toxicol. 19, 23-42 (1988).
    • (1988) CRC Crit. Rev. Toxicol. , vol.19 , pp. 23-42
    • Lock, E.A.1
  • 4
    • 0023546625 scopus 로고
    • Mechanism of transport for toxic cysteine conjugates in rat kidney cortex membrane vesicles
    • V. H. Schaeffer and J. L. Stevens, Mechanism of transport for toxic cysteine conjugates in rat kidney cortex membrane vesicles. Mol. Pharmacol. 32, 293-298 (1987).
    • (1987) Mol. Pharmacol. , vol.32 , pp. 293-298
    • Schaeffer, V.H.1    Stevens, J.L.2
  • 5
    • 0020420551 scopus 로고
    • Organ distribution and biological half-time of methylmercury in four strains of mice
    • R. Doi and T. Kobayashi, Organ distribution and biological half-time of methylmercury in four strains of mice. Jpn. J. Exp. Med. 52, 307-314 (1982).
    • (1982) Jpn. J. Exp. Med. , vol.52 , pp. 307-314
    • Doi, R.1    Kobayashi, T.2
  • 6
    • 0029876769 scopus 로고    scopus 로고
    • Uptake of methylmercury cysteine by rat erythrocytes at lower temperature
    • in press
    • G. Wu, Uptake of methylmercury cysteine by rat erythrocytes at lower temperature. J. Appl. Toxicol. (in press).
    • J. Appl. Toxicol.
    • Wu, G.1
  • 8
    • 0001078989 scopus 로고
    • A package of computer program for pharmacokinetic modeling
    • C. M. Metzler, G. L. Elfring and A. J. McEwen, A package of computer program for pharmacokinetic modeling. Biometrics 30, 562-563 (1974).
    • (1974) Biometrics , vol.30 , pp. 562-563
    • Metzler, C.M.1    Elfring, G.L.2    McEwen, A.J.3
  • 9
    • 0020516344 scopus 로고
    • A study on the biochemical and biological behavior of methylmercury
    • R. Doi and M. Tagawa, A study on the biochemical and biological behavior of methylmercury. Toxicol. Appl. Pharmacol. 69, 407-416 (1983).
    • (1983) Toxicol. Appl. Pharmacol. , vol.69 , pp. 407-416
    • Doi, R.1    Tagawa, M.2
  • 10
    • 0014330798 scopus 로고
    • Mercury compounds in the blood of rats treated with ethylmercuric chloride
    • Y. Takeda, T. Kunugi, T. Terao and T. Ukita, Mercury compounds in the blood of rats treated with ethylmercuric chloride. Toxicol. Appl. Pharmacol 13, 165-173 (1968).
    • (1968) Toxicol. Appl. Pharmacol , vol.13 , pp. 165-173
    • Takeda, Y.1    Kunugi, T.2    Terao, T.3    Ukita, T.4
  • 11
    • 0016207465 scopus 로고
    • Carbon-mercury bond cleavage in blood of rats fed methyl mercuric chloride
    • J. D. Garcia, M. G. Yang, J. H. C. Wang and P. S. Belo, Carbon-mercury bond cleavage in blood of rats fed methyl mercuric chloride. Proc. Soc. Exp. Biol. Med. 146, 66-70 (1974).
    • (1974) Proc. Soc. Exp. Biol. Med. , vol.146 , pp. 66-70
    • Garcia, J.D.1    Yang, M.G.2    Wang, J.H.C.3    Belo, P.S.4
  • 12
    • 0016801860 scopus 로고
    • Effect of selenium on methylmercury binding to subcellular and soluble proteins in rat tissues
    • R. W. Chen, V. L. Lacy and P. D. Whanger, Effect of selenium on methylmercury binding to subcellular and soluble proteins in rat tissues. Res. Commun. Chem. Pathol. Pharmacol. 12, 297-308 (1975).
    • (1975) Res. Commun. Chem. Pathol. Pharmacol. , vol.12 , pp. 297-308
    • Chen, R.W.1    Lacy, V.L.2    Whanger, P.D.3
  • 13
    • 0027293715 scopus 로고
    • The effects of colchicine or vinblastine on the blood calcium level in rats
    • K. Ohya and H. Ogura, The effects of colchicine or vinblastine on the blood calcium level in rats. Eur. J. Pharmacol. 248, 111-119 (1993).
    • (1993) Eur. J. Pharmacol. , vol.248 , pp. 111-119
    • Ohya, K.1    Ogura, H.2
  • 14
    • 0029151051 scopus 로고
    • Effects of inhibitors and substrates on methyl mercury uptake by rat erythrocytes
    • G. Wu, Effects of inhibitors and substrates on methyl mercury uptake by rat erythrocytes. Arch. Toxicol. 69, 533-539 (1995).
    • (1995) Arch. Toxicol. , vol.69 , pp. 533-539
    • Wu, G.1
  • 15
    • 9044231492 scopus 로고
    • Active transport
    • ed. by R. E. Notari, Mercel Dekker, New York
    • R. E. Notari, Active transport. In Biopharmaceutics and Clinical Pharmacokinetics, ed. by R. E. Notari, pp. 37-41. Mercel Dekker, New York (1987).
    • (1987) Biopharmaceutics and Clinical Pharmacokinetics , pp. 37-41
    • Notari, R.E.1
  • 16
    • 0022552179 scopus 로고
    • Active tubular secretion of l-naphthyl-β-D-glucuronide in the isolated perfused rat kidney
    • F. A. M. Redegeld and J. Noordhoek, Active tubular secretion of l-naphthyl-β-D-glucuronide in the isolated perfused rat kidney. Drug Metab. Dispos. 14, 622-624 (1986).
    • (1986) Drug Metab. Dispos. , vol.14 , pp. 622-624
    • Redegeld, F.A.M.1    Noordhoek, J.2
  • 17
    • 0026028088 scopus 로고
    • Nephrotoxicity of the glutathione conjugate of menadione (2-methyl-1,4-naphthoquinone) in the isolated perfused rat kidney: Role of metabolism by γ-glutamyltranspeptidase and probenecid-sensitive transport
    • F. A. M. Redegeld, G. A. Hoffman, P. G. F. Van de Loo, A. S. Koster and J. Noordhoek, Nephrotoxicity of the glutathione conjugate of menadione (2-methyl-1,4-naphthoquinone) in the isolated perfused rat kidney: role of metabolism by γ-glutamyltranspeptidase and probenecid-sensitive transport. J. Pharmacol. Exp. Ther. 256, 665-669 (1991).
    • (1991) J. Pharmacol. Exp. Ther. , vol.256 , pp. 665-669
    • Redegeld, F.A.M.1    Hoffman, G.A.2    Van de Loo, P.G.F.3    Koster, A.S.4    Noordhoek, J.5
  • 18
    • 0020265930 scopus 로고
    • Metabolic coordination of liver and kidney in mercapturic acid biosynthesis in vivo
    • M. Inoue, K. Okajima and Y. Morino, Metabolic coordination of liver and kidney in mercapturic acid biosynthesis in vivo. Hepatology 2, 572-579 (1982).
    • (1982) Hepatology , vol.2 , pp. 572-579
    • Inoue, M.1    Okajima, K.2    Morino, Y.3
  • 19
    • 0026725202 scopus 로고
    • Routes for renal transport of methylmercury in mice
    • T. Tanaka, A. Naganuma and N. Imura, Routes for renal transport of methylmercury in mice. Eur. J. Pharmacol. 228, 9-14 (1992).
    • (1992) Eur. J. Pharmacol. , vol.228 , pp. 9-14
    • Tanaka, T.1    Naganuma, A.2    Imura, N.3
  • 20
    • 0026510944 scopus 로고
    • ATP-dependent multispecific organic anion transport system in rat erythrocyte membrane vesicles
    • M. Heijn, R. P. J. Oude Elferink and P. L. M. Jansen, ATP-dependent multispecific organic anion transport system in rat erythrocyte membrane vesicles. Am. J. Physiol. 262, C104-C110 (1992).
    • (1992) Am. J. Physiol. , vol.262
    • Heijn, M.1    Oude Elferink, R.P.J.2    Jansen, P.L.M.3
  • 21
    • 0024430157 scopus 로고
    • Anisosmotic cell volume regulation: A comparative view
    • M. E. Chamberlin and K. Strange, Anisosmotic cell volume regulation: a comparative view. Am. J. Physiol. 257, C159-C173 (1989).
    • (1989) Am. J. Physiol. , vol.257
    • Chamberlin, M.E.1    Strange, K.2
  • 22
    • 0024594966 scopus 로고
    • Membrane mechanisms in volume and pH regulation in vertebrate cells
    • E. K. Hoffmann and L. O. Simonsen, Membrane mechanisms in volume and pH regulation in vertebrate cells. Physiol. Rev. 69, 315-382 (1989).
    • (1989) Physiol. Rev. , vol.69 , pp. 315-382
    • Hoffmann, E.K.1    Simonsen, L.O.2
  • 23
    • 0000587593 scopus 로고
    • The role of organic osmolytes in the regulation of mammalian cell volume
    • ed. by R. Gilles, Springer-Verlag, Berfin
    • R. O. Law and M. B. Burg, The role of organic osmolytes in the regulation of mammalian cell volume. In Advances in Comparative and Environmental Physiology, ed. by R. Gilles, Vol. 9, pp. 189-225. Springer-Verlag, Berfin (1991).
    • (1991) Advances in Comparative and Environmental Physiology , vol.9 , pp. 189-225
    • Law, R.O.1    Burg, M.B.2
  • 24
    • 0022350184 scopus 로고
    • - cotransport: Sulfhydryls, divalent cations, and the mechanism of volume activation in a red cells
    • - cotransport: sulfhydryls, divalent cations, and the mechanism of volume activation in a red cells. J. Membr. Biol. 88, 1-13 (1985).
    • (1985) J. Membr. Biol. , vol.88 , pp. 1-13
    • Lauf, P.K.1
  • 25
    • 0017744866 scopus 로고
    • Effect of temperature and of cytochalasin B and persantin on the nonmediated permeation of non-electrolytes into cultured Novikoff rat hepatoma cells
    • J. C. Graft, R. M. Wohlhueter and G. W. Plagemann, Effect of temperature and of cytochalasin B and persantin on the nonmediated permeation of non-electrolytes into cultured Novikoff rat hepatoma cells. J. Biol, Chem. 252, 4185-4190 (1977).
    • (1977) J. Biol, Chem. , vol.252 , pp. 4185-4190
    • Graft, J.C.1    Wohlhueter, R.M.2    Plagemann, G.W.3
  • 26
    • 0018179682 scopus 로고
    • Specificity of the effects of cytochalasin B on transport and motile processes
    • S. Lin, D. C. Lin and M. D. Flanagan, Specificity of the effects of cytochalasin B on transport and motile processes. Proc. Natl. Acad. Sci. USA 75, 329-333 (1978).
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 329-333
    • Lin, S.1    Lin, D.C.2    Flanagan, M.D.3
  • 27
    • 0023241981 scopus 로고
    • Binding of cytochalasin B to trypsin and thermolysin fragments of the human erythrocyte hexose transporter
    • A. R. Karim, W. D. Rees and G. D. Holman, Binding of cytochalasin B to trypsin and thermolysin fragments of the human erythrocyte hexose transporter. Biochim. Biophys. Acta 902, 402-405 (1987).
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 402-405
    • Karim, A.R.1    Rees, W.D.2    Holman, G.D.3
  • 28
    • 0027489321 scopus 로고
    • Tryptic digestion of the human erythrocyte glucose transporter: Effects on ligand binding and tryptophan fluorescence
    • J. M. May, Q. Zhi-chao and J. M. Beechem, Tryptic digestion of the human erythrocyte glucose transporter: effects on ligand binding and tryptophan fluorescence. Biochemistry 32, 9524-9531 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9524-9531
    • May, J.M.1    Zhi-chao, Q.2    Beechem, J.M.3
  • 29
    • 0021871717 scopus 로고
    • +-activated adenosine triphosphatase system
    • +-activated adenosine triphosphatase system. Biochem. J. 227, 1-11 (1985).
    • (1985) Biochem. J. , vol.227 , pp. 1-11
    • Anner, B.M.1
  • 31
    • 0027197566 scopus 로고
    • Ouabain causes kaliuresis and work synergistically with aldosterone in vivo
    • H. Sekihara and Y. Yazaki, Ouabain causes kaliuresis and work synergistically with aldosterone in vivo. Life Sci. 53, 975-980 (1993).
    • (1993) Life Sci. , vol.53 , pp. 975-980
    • Sekihara, H.1    Yazaki, Y.2
  • 32
    • 0022225769 scopus 로고
    • Effect of fluoride on retinal rod outer segment cGMP phosphodiesterase and G-protein
    • N. J. Cook, G. Nullans and N. Virmaux, Effect of fluoride on retinal rod outer segment cGMP phosphodiesterase and G-protein. Biochem. Biophys. Res. Commun. 131, 146-151 (1985).
    • (1985) Biochem. Biophys. Res. Commun. , vol.131 , pp. 146-151
    • Cook, N.J.1    Nullans, G.2    Virmaux, N.3
  • 33
    • 0022583875 scopus 로고
    • Further evidence for a phosphoplipase C-coupled G-protein in hamster fibrobiasts. (Induction of inositol phosphates formation by fluoaluminate and vanadate and inhibition by pertussis toxin)
    • S. Paris and J. Pauyssegur, Further evidence for a phosphoplipase C-coupled G-protein in hamster fibrobiasts. (Induction of inositol phosphates formation by fluoaluminate and vanadate and inhibition by pertussis toxin). EMBO J. 5, 55-60 (1986).
    • (1986) EMBO J. , vol.5 , pp. 55-60
    • Paris, S.1    Pauyssegur, J.2
  • 34
    • 0023035856 scopus 로고
    • Use of fluoride ion as a probe for the guanine nucleotide-binding protein involved in the phosphoinositide-depertdent neutrophil transduction pathway
    • C. F. Strand, J. E. Parente and K. Wong, Use of fluoride ion as a probe for the guanine nucleotide-binding protein involved in the phosphoinositide-depertdent neutrophil transduction pathway. FEBS Lett. 206, 20-24 (1986).
    • (1986) FEBS Lett. , vol.206 , pp. 20-24
    • Strand, C.F.1    Parente, J.E.2    Wong, K.3
  • 35
    • 0021823386 scopus 로고
    • Effect of NaF on rat parotid gland amyfase activity and cAMP concentration in vitro and in vivo
    • A. R. Shahed, J. Bondi and D. W. Allmann, Effect of NaF on rat parotid gland amyfase activity and cAMP concentration in vitro and in vivo. J. Dent. Res. 64, 1126-1129 (1985).
    • (1985) J. Dent. Res. , vol.64 , pp. 1126-1129
    • Shahed, A.R.1    Bondi, J.2    Allmann, D.W.3
  • 37
    • 0027494618 scopus 로고
    • Human erythrocyte membrane lipid asymmetry-transbilayer distribution of rapidly diffusing phosphatidylserines
    • R. K. Loh and W. H. Huestis, Human erythrocyte membrane lipid asymmetry-transbilayer distribution of rapidly diffusing phosphatidylserines. Biochemistry 32, 11722-11726 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11722-11726
    • Loh, R.K.1    Huestis, W.H.2
  • 38
    • 0022428478 scopus 로고
    • Primary structure and transmembrane orientation of the murine anion exchange protein
    • R. R. Kopito and H. F. Lodish, Primary structure and transmembrane orientation of the murine anion exchange protein. Nature 316, 234-238 (1985).
    • (1985) Nature , vol.316 , pp. 234-238
    • Kopito, R.R.1    Lodish, H.F.2
  • 39
    • 0027325804 scopus 로고
    • +-dependent sulfate transport in opossum kidney cells is DIDS sensitive
    • +-dependent sulfate transport in opossum kidney cells is DIDS sensitive. Am. J. Physiol. 265, C54-C61 (1993).
    • (1993) Am. J. Physiol. , vol.265
    • Tenenhouse, H.S.1    Martel, J.2
  • 40
    • 4243930326 scopus 로고
    • + transport in rabbit red blood cells: Comparison with oxygenated human SS cells
    • + transport in rabbit red blood cells: comparison with oxygenated human SS cells. Am. J. Physiol. 157, C114-C121 (1989).
    • (1989) Am. J. Physiol. , vol.157
    • Ai-Rohil, N.1    Jennings, M.L.2
  • 42
    • 0018884541 scopus 로고
    • + flux induced by N-ethylmaleimide in genetically low K sheep and goat erythrocytes
    • + flux induced by N-ethylmaleimide in genetically low K sheep and goat erythrocytes. Biochem. Biophys. Res. Commun. 93, 1422-1428 (1980).
    • (1980) Biochem. Biophys. Res. Commun. , vol.93 , pp. 1422-1428
    • Lauf, P.K.1    Theg, B.E.2
  • 43
    • 0344504714 scopus 로고
    • Passive potassium transport in LK sheep red cells. Modification by N-ethylmaleimide
    • P. Logue, C. Anderson, C. Kanik, B. Farquharson and P. B. Dunham, Passive potassium transport in LK sheep red cells. Modification by N-ethylmaleimide. J. Gen. Physiol. 81, 8861-8885 (1985).
    • (1985) J. Gen. Physiol. , vol.81 , pp. 8861-8885
    • Logue, P.1    Anderson, C.2    Kanik, C.3    Farquharson, B.4    Dunham, P.B.5
  • 44
    • 0021365942 scopus 로고
    • Effect of volume changes on ouabain-insensittve net outward cation movements in human red cells
    • N. C. Adragna and D. C. Tosteson, Effect of volume changes on ouabain-insensittve net outward cation movements in human red cells. J. Membr. Biol. 78, 43-52 (1984).
    • (1984) J. Membr. Biol. , vol.78 , pp. 43-52
    • Adragna, N.C.1    Tosteson, D.C.2
  • 45
    • 0026803302 scopus 로고
    • Increase of apamin receptors in skeletal muscle induced by axonal flow blockers
    • M. I. Bahrens and C. Vergara, Increase of apamin receptors in skeletal muscle induced by axonal flow blockers. Am. J. Physiol. 263, C794-C802 (1992).
    • (1992) Am. J. Physiol. , vol.263
    • Bahrens, M.I.1    Vergara, C.2
  • 46
    • 0020404847 scopus 로고
    • Potential mechanisms underlying the destruction of dentate gyrus granule cells by colchicine
    • E. W. Lothman, D. A. Stein, G. F. Wooten and D. K. Zucker, Potential mechanisms underlying the destruction of dentate gyrus granule cells by colchicine. Exp. Neurol. 78, 293-302 (1982).
    • (1982) Exp. Neurol. , vol.78 , pp. 293-302
    • Lothman, E.W.1    Stein, D.A.2    Wooten, G.F.3    Zucker, D.K.4
  • 47
    • 0027504394 scopus 로고
    • Extracellular recordings in the colchicine-lesioned rat dentate gyrus following transplants of fetal dentate gyrus and CA1 hippocampal subfield tissue
    • G. S. Dawe, J. A. Gray, J. D. Sinden, J. D. Stephenson and M. Segal, Extracellular recordings in the colchicine-lesioned rat dentate gyrus following transplants of fetal dentate gyrus and CA1 hippocampal subfield tissue. Brain Res. 625, 63-74 (1993).
    • (1993) Brain Res. , vol.625 , pp. 63-74
    • Dawe, G.S.1    Gray, J.A.2    Sinden, J.D.3    Stephenson, J.D.4    Segal, M.5
  • 48
    • 0019167194 scopus 로고
    • A colchicine-sensitive uptake system in Morris hepatomas
    • R. Tauber and W. Reutter, A colchicine-sensitive uptake system in Morris hepatomas. Proc. Natl. Acad. Sci. USA 77, 5282-5286 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5282-5286
    • Tauber, R.1    Reutter, W.2
  • 49
    • 0020283865 scopus 로고
    • Uptake of methylmercury and inorganic mercury by mouse glioma and mouse neuroblastoma cells
    • S. Nakada and N. Imura, Uptake of methylmercury and inorganic mercury by mouse glioma and mouse neuroblastoma cells. Neurotoxicology 3, 249-258 (1982).
    • (1982) Neurotoxicology , vol.3 , pp. 249-258
    • Nakada, S.1    Imura, N.2
  • 50
    • 0021214204 scopus 로고
    • Microtubule modulation of biliary excretion of endogenous and exogenous hepatic lysosomal constituents
    • R. B. Swell, S. S. Barham, A. R. Zinsmeister and N. F. LaRusso, Microtubule modulation of biliary excretion of endogenous and exogenous hepatic lysosomal constituents. Am. J. Physiol. 246, G8-G15 (1984).
    • (1984) Am. J. Physiol. , vol.246
    • Swell, R.B.1    Barham, S.S.2    Zinsmeister, A.R.3    LaRusso, N.F.4
  • 51
    • 0018218555 scopus 로고
    • Effects of methylmercury on mitotic mouse glioma cells
    • K. Miura, K. Suzuki and N. Imura, Effects of methylmercury on mitotic mouse glioma cells. Environ. Res. 17, 453-471 (1978).
    • (1978) Environ. Res. , vol.17 , pp. 453-471
    • Miura, K.1    Suzuki, K.2    Imura, N.3
  • 52
    • 0019174603 scopus 로고
    • Mechanism of methylmercury cytotoxicity: By biochemical and morphological experiment using cultured cells
    • N. Imura, K. Miura, M. Inokawa and S. Nakada, Mechanism of methylmercury cytotoxicity: by biochemical and morphological experiment using cultured cells. Toxicology 17, 241-254 (1980).
    • (1980) Toxicology , vol.17 , pp. 241-254
    • Imura, N.1    Miura, K.2    Inokawa, M.3    Nakada, S.4
  • 53
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals. Distribution of homocysteine between competing pathways
    • J. D. Finkelstein and J. J. Martin, Methionine metabolism in mammals. Distribution of homocysteine between competing pathways. J. Biol. Chem. 259, 9508-9513 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 54
    • 0022464168 scopus 로고
    • Metabolism of sulfur-containing amino acid
    • M. H. Stipanuk, Metabolism of sulfur-containing amino acid. Annu. Rev. Natr. 6, 179-209 (1986).
    • (1986) Annu. Rev. Natr. , vol.6 , pp. 179-209
    • Stipanuk, M.H.1
  • 55
    • 0020078507 scopus 로고
    • Discrimination of three parallel pathways of lactate transport in the human erythrocyte membrane by inhibitors and kinetic properties
    • B. Deuticke, E. Beyer and B. Forst, Discrimination of three parallel pathways of lactate transport in the human erythrocyte membrane by inhibitors and kinetic properties. Biochim. Biophys. Acta 684, 96-110 (1982).
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 96-110
    • Deuticke, B.1    Beyer, E.2    Forst, B.3


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