메뉴 건너뛰기




Volumn 31, Issue 1, 1999, Pages 61-70

Differential response of non-transferrin bound iron uptake in rat liver cells on long-term and short-term treatment with iron

Author keywords

Ferrocene; Iron overload; Iron uptake; Non transferrin bound iron; Rat liver

Indexed keywords

DEFEROXAMINE; FERRIC AMMONIUM CITRATE; FERRIC CITRATE; FERROCENE DERIVATIVE; IRON; IRON DERIVATIVE; IRON REGULATORY FACTOR; PENTETIC ACID; TRANSFERRIN;

EID: 0032992695     PISSN: 01688278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-8278(99)80164-0     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 0023037399 scopus 로고
    • Crichton RR An animal model of iron overload and its application to study hepatic ferritin iron mobilization by chelators
    • Longueville A. Crichton RR An animal model of iron overload and its application to study hepatic ferritin iron mobilization by chelators. Biochem Pharmacol. 35:1986;3669-3678.
    • (1986) Biochem Pharmacol , vol.35 , pp. 3669-3678
    • Longueville, A.1
  • 2
    • 0026088232 scopus 로고
    • Biochemical and biophysical investigations of the ferrocene-iron-loaded rat. An animal model of primary haemochromatosis
    • Ward RJ, Florence AL, Baldwin D, Abiaka C, Roland F, Ramsey MH, et al. Biochemical and biophysical investigations of the ferrocene-iron-loaded rat. An animal model of primary haemochromatosis. Eur J Biochem. 202:1991;405-410.
    • (1991) Eur J Biochem , vol.202 , pp. 405-410
    • Ward, R.J.1    Florence, A.L.2    Baldwin, D.3    Abiaka, C.4    Roland, F.5    Ramsey, M.H.6
  • 3
    • 0026698175 scopus 로고
    • Studies of in vivo iron mobilization by chelators in the ferrocene-loaded rat
    • Florence A, Ward RJ, Peters TJ, Crichton RR. Studies of in vivo iron mobilization by chelators in the ferrocene-loaded rat. Biochem Pharmacol. 44:1992;1023-1027.
    • (1992) Biochem Pharmacol , vol.44 , pp. 1023-1027
    • Florence, A.1    Ward, R.J.2    Peters, T.J.3    Crichton, R.R.4
  • 4
    • 0028920115 scopus 로고
    • Nielsen P Ethane exhalation and vitamin E/ubiquinol status as markers of lipid peroxidation in ferrocene iron-loaded rats
    • Dresow B, Albert C, Zimmermann I. Nielsen P Ethane exhalation and vitamin E/ubiquinol status as markers of lipid peroxidation in ferrocene iron-loaded rats. Hepatology. 21:1995;1099-1105.
    • (1995) Hepatology , vol.21 , pp. 1099-1105
    • Dresow, B.1    Albert, C.2    Zimmermann, I.3
  • 5
    • 0023007268 scopus 로고
    • Characterization of non-transferrin bound iron clearance by rat liver
    • Wright TL, Brissot P, Ma W-L, Weisiger RA. Characterization of non-transferrin bound iron clearance by rat liver. J Biol Chem. 261:1986;10909-10914.
    • (1986) J Biol Chem , vol.261 , pp. 10909-10914
    • Wright, T.L.1    Brissot, P.2    Ma W-L3    Weisiger, R.A.4
  • 6
    • 0023931434 scopus 로고
    • Non-transferrin-bound iron uptake by the liver Role of membrane potential difference
    • Wright TL, Fitz JG, Weisiger RA. Non-transferrin-bound iron uptake by the liver Role of membrane potential difference. J Biol Chem. 263:1988;1842-1847.
    • (1988) J Biol Chem , vol.263 , pp. 1842-1847
    • Wright, T.L.1    Fitz, J.G.2    Weisiger, R.A.3
  • 7
    • 0022345593 scopus 로고
    • Efficient clearance of nontransferrin-bound iron by rat liver
    • Brissot P, Wright TL, Weisiger RA. Efficient clearance of nontransferrin-bound iron by rat liver. J Clin Invest. 76:1985;1463-1470.
    • (1985) J Clin Invest , vol.76 , pp. 1463-1470
    • Brissot, P.1    Wright, T.L.2    Weisiger, R.A.3
  • 8
    • 0025133292 scopus 로고
    • Mechanisms of transport of nontransferrin-bound iron in basolateral and canalicular rat liver plasma membrane vesicles
    • Wright TL, Lake JR. Mechanisms of transport of nontransferrin-bound iron in basolateral and canalicular rat liver plasma membrane vesicles. Hepatology. 12:1990;498-504.
    • (1990) Hepatology , vol.12 , pp. 498-504
    • Wright, T.L.1    Lake Jr2
  • 9
    • 0024564712 scopus 로고
    • Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis: Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy
    • Grootveld M, Bell JD, Halliwell B, Aruoma OJ, Bomford A, Sadler PJ. Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis: characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy. J Biol Chem. 264:1989;4417-4422.
    • (1989) J Biol Chem , vol.264 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Aruoma, O.J.4    Bomford, A.5    Sadler, P.J.6
  • 10
    • 0030026267 scopus 로고    scopus 로고
    • Uptake of iron by isolated rat hepatocytes from a hydrophilic impermeant ferric chelate, Fe(III)DTPA
    • Scheiber B, Goldenberg H. Uptake of iron by isolated rat hepatocytes from a hydrophilic impermeant ferric chelate, Fe(III)DTPA. Arch Biochem Biophys. 326:1996;185-192.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 185-192
    • Scheiber, B.1    Goldenberg, H.2
  • 11
    • 0028832455 scopus 로고
    • Evidence for a low K-m transporter for non-transferrin-bound iron in isolated rat hepatocytes
    • Barisani D, Berg CL, Wessling-Resnick M, Gollan JL. Evidence for a low K-m transporter for non-transferrin-bound iron in isolated rat hepatocytes. Am J Physiol. 26:1995;G570-G576.
    • (1995) Am J Physiol , vol.26
    • Barisani, D.1    Berg, C.L.2    Wessling-Resnick, M.3    Gollan, J.L.4
  • 12
    • 0032053475 scopus 로고    scopus 로고
    • Ferric citrate uptake by cultured rat hepatocytes is inhibited in the presence of transferrin
    • Graham RM, Morgan EH, Baker E. Ferric citrate uptake by cultured rat hepatocytes is inhibited in the presence of transferrin. Eur J Biochem. 253:1998;139-145.
    • (1998) Eur J Biochem , vol.253 , pp. 139-145
    • Graham, R.M.1    Morgan, E.H.2    Baker, E.3
  • 13
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal ion transporter
    • Gunshin H, Mackenzie B, Berger UV, Gunshin Y, Romero MF, Boron WF, et al. Cloning and characterization of a mammalian proton-coupled metal ion transporter. Nature. 388:1997;482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6
  • 14
    • 0032477866 scopus 로고    scopus 로고
    • Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming MD, Romano MA, Su MA, Garrick LM, Garrick MD, Andrews NC. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc Natl Acad Sci. 95:1998;1148-1153.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 1148-1153
    • Fleming, M.D.1    Romano Ma2    Su Ma3    Garrick, L.M.4    Garrick, M.D.5    Andrews, N.C.6
  • 15
    • 0032516881 scopus 로고    scopus 로고
    • Structural and functional analysis of SFT, a stimulator of Fe Transport
    • Yu J, Wessling-Resnick M. Structural and functional analysis of SFT, a stimulator of Fe Transport. J Biol Chem. 273:1998;21380-21385.
    • (1998) J Biol Chem , vol.273 , pp. 21380-21385
    • Yu, J.1    Wessling-Resnick, M.2
  • 16
    • 0026673757 scopus 로고
    • Coordination of cellular iron metabolism by post-transcriptional gene regulation
    • Kühn LC, Hentze MW. Coordination of cellular iron metabolism by post-transcriptional gene regulation. J Inorg Biochem. 47:1992;183-195.
    • (1992) J Inorg Biochem , vol.47 , pp. 183-195
    • Kühn, L.C.1    Hentze, M.W.2
  • 17
    • 0027452550 scopus 로고
    • Regulating the fate of messenger RNA - The control of cellular iron metabolism
    • Klausner RD, Rouault TA, Harford JB. Regulating the fate of messenger RNA - the control of cellular iron metabolism. Cell. 72:1993;19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 18
    • 0025774978 scopus 로고
    • Regulation of the transferrin-independent iron transport system in cultured cells
    • Kaplan J, Jordan I, Sturrock A. Regulation of the transferrin-independent iron transport system in cultured cells. J Biol Chem. 266:1991;2997-3004.
    • (1991) J Biol Chem , vol.266 , pp. 2997-3004
    • Kaplan, J.1    Jordan, I.2    Sturrock, A.3
  • 19
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells - The effect of desferrioxamine and ferric ammonium citrate
    • Richardson D, Baker E. Two mechanisms of iron uptake from transferrin by melanoma cells - the effect of desferrioxamine and ferric ammonium citrate. J Biol Chem. 267:1992;13972-13979.
    • (1992) J Biol Chem , vol.267 , pp. 13972-13979
    • Richardson, D.1    Baker, E.2
  • 20
    • 0026506416 scopus 로고
    • Non-transferrin dependent Fe-59 uptake in phytohemagglutinin-stimulated human peripheral lymphocytes
    • Hamazaki S, Glass J. Non-transferrin dependent Fe-59 uptake in phytohemagglutinin-stimulated human peripheral lymphocytes. Exp Hematol. 20:1992;436-441.
    • (1992) Exp Hematol , vol.20 , pp. 436-441
    • Hamazaki, S.1    Glass, J.2
  • 21
    • 0026598837 scopus 로고
    • The effect of desferrioxamine and ferric ammonium citrate on the uptake of iron by the membrane iron- binding component of human melanoma cells
    • Richardson DR, Baker E. The effect of desferrioxamine and ferric ammonium citrate on the uptake of iron by the membrane iron- binding component of human melanoma cells. Biochim Biophys Acta. 1103:1992;275-280.
    • (1992) Biochim Biophys Acta , vol.1103 , pp. 275-280
    • Richardson, D.R.1    Baker, E.2
  • 22
    • 0027512915 scopus 로고
    • Characterization of transferrinindependent iron transport in K562 cells - unique properties provide evidence for multiple pathways of iron uptake
    • Inman RS, Wessling-Resnick M. Characterization of transferrinindependent iron transport in K562 cells - unique properties provide evidence for multiple pathways of iron uptake. J Biol Chem. 268:1993;8521-8528.
    • (1993) J Biol Chem , vol.268 , pp. 8521-8528
    • Inman, R.S.1    Wessling-Resnick, M.2
  • 23
    • 0027313329 scopus 로고
    • Effects of iron loading on uptake, speciation, and chelation of iron in cultured myocardial cells
    • Parkes JG, Hussain RA, Olivieri NF, Templeton DM. Effects of iron loading on uptake, speciation, and chelation of iron in cultured myocardial cells. J Lab Clin Med. 122:1993;36-47.
    • (1993) J Lab Clin Med , vol.122 , pp. 36-47
    • Parkes, J.G.1    Hussain, R.A.2    Olivieri, N.F.3    Templeton, D.M.4
  • 24
    • 84945734134 scopus 로고
    • Non-transferrin iron uptake by HeLa cells cultured in serumfree media with different sources of iron supply
    • Kriegerbeckova K, Döpper L, Scheiber B, Kovar J, Goldenberg H. Non-transferrin iron uptake by HeLa cells cultured in serumfree media with different sources of iron supply. Eur J Clin Chem Clin Biochem. 33:1995;791-797.
    • (1995) Eur J Clin Chem Clin Biochem , vol.33 , pp. 791-797
    • Kriegerbeckova, K.1    Döpper, L.2    Scheiber, B.3    Kovar, J.4    Goldenberg, H.5
  • 25
    • 0025151812 scopus 로고
    • Effect of cellular iron concentration on iron uptake by hepatocytes
    • Trinder D, Batey RG, Morgan EH, Baker E. Effect of cellular iron concentration on iron uptake by hepatocytes. Am J Physiol. 259:1990;G611-G617.
    • (1990) Am J Physiol , vol.259
    • Trinder, D.1    Batey, R.G.2    Morgan, E.H.3    Baker, E.4
  • 26
    • 0027959626 scopus 로고
    • Iron transport and subcellular distribution in HepG2 hepatocarcinoma cells
    • Parkes JG, Templeton DM. Iron transport and subcellular distribution in HepG2 hepatocarcinoma cells. Ann Clin Lab Sci. 24:1994;509-520.
    • (1994) Ann Clin Lab Sci , vol.24 , pp. 509-520
    • Parkes, J.G.1    Templeton, D.M.2
  • 27
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • Randell EW, Parkes JG, Olivieri NF, Templeton DM. Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron. J Biol Chem. 269:1994;16046-16053.
    • (1994) J Biol Chem , vol.269 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 28
    • 0028933888 scopus 로고
    • Templeton DM Modulation by iron loading and chelation of the uptake of non transferrin bound iron by human liver cells
    • Parkes JG, Randell EW, Olivieri NF. Templeton DM Modulation by iron loading and chelation of the uptake of non transferrin bound iron by human liver cells. Biochim Biophys Acta. 1243:1995;373-380.
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 373-380
    • Parkes, J.G.1    Randell, E.W.2    Olivieri, N.F.3
  • 29
    • 0028875152 scopus 로고
    • Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction
    • Richardson DR, Ponka P. Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction. Biochim Biophys Acta. 1269:1995;105-114.
    • (1995) Biochim Biophys Acta , vol.1269 , pp. 105-114
    • Richardson, D.R.1    Ponka, P.2
  • 30
    • 0026632436 scopus 로고
    • Regulatory effects of gallium on transferrin- independent iron uptake by human leukemic HL60 cells
    • Chitambar CR, Sax D. Regulatory effects of gallium on transferrin- independent iron uptake by human leukemic HL60 cells. Blood. 80:1992;505-511.
    • (1992) Blood , vol.80 , pp. 505-511
    • Chitambar, C.R.1    Sax, D.2
  • 31
    • 0031035326 scopus 로고    scopus 로고
    • Polyvalent cationic metals induce the rate of transferrin independent iron acquisition by HL60 cells
    • Olakanmi O, Stokes JB, Pathan S, Britigan BE. Polyvalent cationic metals induce the rate of transferrin independent iron acquisition by HL60 cells. J Biol Chem. 272:1997;2599-2606.
    • (1997) J Biol Chem , vol.272 , pp. 2599-2606
    • Olakanmi, O.1    Stokes, J.B.2    Pathan, S.3    Britigan, B.E.4
  • 32
    • 0032579397 scopus 로고    scopus 로고
    • Role of ceruloplasmin in cellular iron uptake
    • Mukhopadhyay CK, Attieh ZK, Fox PL. Role of ceruloplasmin in cellular iron uptake. Science. 279:1998;714-717.
    • (1998) Science , vol.279 , pp. 714-717
    • Mukhopadhyay, C.K.1    Attieh, Z.K.2    Fox, P.L.3
  • 33
    • 0027473840 scopus 로고
    • Metabolism of iron from (3,5,5,-trimetylhexanoyl) ferrocene in rats. A dietary model for severe iron overload
    • Nielsen P, Heinrich HC. Metabolism of iron from (3,5,5,-trimetylhexanoyl) ferrocene in rats. A dietary model for severe iron overload. Biochem Pharmacol. 45:1993;385-391.
    • (1993) Biochem Pharmacol , vol.45 , pp. 385-391
    • Nielsen, P.1    Heinrich, H.C.2
  • 34
    • 0027435650 scopus 로고
    • Chronic feeding of carbonyliron and TMH-ferrocene in rats. Comparison of two iron-over-loaded models
    • Nielsen P, Heinzel S, Düllmann J. Chronic feeding of carbonyliron and TMH-ferrocene in rats. Comparison of two iron-over-loaded models. Comp Biochem Physiol. 106C:1993;429-436.
    • (1993) Comp Biochem Physiol , vol.106 C , pp. 429-436
    • Nielsen, P.1    Heinzel, S.2    Düllmann, J.3
  • 35
    • 0017101039 scopus 로고
    • Preparation of isolated rat liver cells
    • Seglen PO. Preparation of isolated rat liver cells. Methods Cell Biol. 13:1976;29-83.
    • (1976) Methods Cell Biol , vol.13 , pp. 29-83
    • Seglen, P.O.1
  • 36
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall E, Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer. 20:1977;1-5.
    • (1977) Int J Cancer , vol.20 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 37
    • 0031924505 scopus 로고    scopus 로고
    • The surface of rat hepatocytes can transfer iron from stable chelates to external acceptors
    • Scheiber B, Goldenberg H. The surface of rat hepatocytes can transfer iron from stable chelates to external acceptors. Hepatology. 27:1998;1075-1080.
    • (1998) Hepatology , vol.27 , pp. 1075-1080
    • Scheiber, B.1    Goldenberg, H.2
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 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
  • 39
    • 0026007152 scopus 로고
    • Effects of calcium on hepatocyte iron uptake from transferrin, iron-pyrophosphate and iron-ascorbate
    • Nilsen T. Effects of calcium on hepatocyte iron uptake from transferrin, iron-pyrophosphate and iron-ascorbate. Biochim Biophys Acta. 1095:1991;39-45.
    • (1991) Biochim Biophys Acta , vol.1095 , pp. 39-45
    • Nilsen, T.1
  • 40
    • 0032510294 scopus 로고    scopus 로고
    • Characterisation of non-transferrin-bound iron (ferric citrate) uptake by rat hepatocytes in culture
    • Baker E, Baker SM, Morgan EH. Characterisation of non-transferrin-bound iron (ferric citrate) uptake by rat hepatocytes in culture. Biochim Biophys Acta. 1380:1998;21-30.
    • (1998) Biochim Biophys Acta , vol.1380 , pp. 21-30
    • Baker, E.1    Baker, S.M.2    Morgan, E.H.3
  • 41
    • 0028209786 scopus 로고
    • Role of membrane surface potential and other factors in the uptake of non-transferrin-bound iron by reticulocytes
    • Quail EA, Morgan EH. Role of membrane surface potential and other factors in the uptake of non-transferrin-bound iron by reticulocytes. J Cell Physiol. 159:1994;238-244.
    • (1994) J Cell Physiol , vol.159 , pp. 238-244
    • Quail, E.A.1    Morgan, E.H.2
  • 42
    • 0029980050 scopus 로고    scopus 로고
    • Iron transport into erythroid cells by the Na+/Mg2+ antiport
    • Stonell LM, Savigni DL, Morgan EH. Iron transport into erythroid cells by the Na+/Mg2+ antiport. Biochim Biophys Acta. 1282:1996;163-170.
    • (1996) Biochim Biophys Acta , vol.1282 , pp. 163-170
    • Stonell, L.M.1    Savigni, D.L.2    Morgan, E.H.3
  • 43
    • 0021296816 scopus 로고
    • Transferrin and iron uptake by rat hepatocytes in culture
    • Page M, Baker E, Morgan EH. Transferrin and iron uptake by rat hepatocytes in culture. Am J Physiol. 246:1984;G26-G33.
    • (1984) Am J Physiol , vol.246
    • Page, M.1    Baker, E.2    Morgan, E.H.3
  • 44
    • 0026894803 scopus 로고
    • Hepatic heparan sulfate proteoglycan and the recycling of transferrin
    • Hu W-L, Regoeczi E. Hepatic heparan sulfate proteoglycan and the recycling of transferrin. Biochem Cell Biol. 70:1992;535-538.
    • (1992) Biochem Cell Biol , vol.70 , pp. 535-538
    • Hu W-L1    Regoeczi, E.2
  • 45
    • 0029152149 scopus 로고
    • Uptake of iron from N-terminal half transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor independent iron uptake
    • Thorstensen K, Trinder D, Zak O, Aisen P. Uptake of iron from N-terminal half transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor independent iron uptake. Eur J Biochem. 232:1995;129-133.
    • (1995) Eur J Biochem , vol.232 , pp. 129-133
    • Thorstensen, K.1    Trinder, D.2    Zak, O.3    Aisen, P.4
  • 46
    • 0029953577 scopus 로고    scopus 로고
    • Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression
    • Trinder D, Zak O, Aisen P. Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression. Hepatology. 23:1996;1512-1520.
    • (1996) Hepatology , vol.23 , pp. 1512-1520
    • Trinder, D.1    Zak, O.2    Aisen, P.3
  • 47
    • 0030761075 scopus 로고    scopus 로고
    • Inhibition of uptake of transferrin-bound iron by human hepatoma cells by non-transferrin bound iron
    • Trinder D, Morgan E. Inhibition of uptake of transferrin-bound iron by human hepatoma cells by non-transferrin bound iron. Hepatology. 26:1997;691-698.
    • (1997) Hepatology , vol.26 , pp. 691-698
    • Trinder, D.1    Morgan, E.2
  • 48
    • 0029832659 scopus 로고    scopus 로고
    • Fe-nitrilotriacetic acid-binding proteins associated with rat liver plasma membranes
    • Barisani D, Wessling-Resnick M. Fe-nitrilotriacetic acid-binding proteins associated with rat liver plasma membranes. Hepatology. 24:1996;934-938.
    • (1996) Hepatology , vol.24 , pp. 934-938
    • Barisani, D.1    Wessling-Resnick, M.2
  • 50
    • 0028793251 scopus 로고
    • Isolated hepatocytes acquire iron from lactoferrin by endocytosis
    • McAbee DD. Isolated hepatocytes acquire iron from lactoferrin by endocytosis. Biochem J. 311:1995;603-609.
    • (1995) Biochem J , vol.311 , pp. 603-609
    • McAbee, D.D.1
  • 51
    • 0015217866 scopus 로고
    • The kinetics and mechanism of iron(III) exchange between chelates and transferrin: IV. The reaction of transferrin with iron(III) nitrilotriacetate
    • Bates GW, Wernicke J. The kinetics and mechanism of iron(III) exchange between chelates and transferrin: IV. The reaction of transferrin with iron(III) nitrilotriacetate. J Biol Chem. 246:1971;3679-3685.
    • (1971) J Biol Chem , vol.246 , pp. 3679-3685
    • Bates, G.W.1    Wernicke, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.