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Volumn 68, Issue 1-2, 1999, Pages 65-75

Purification and identification of an estrogen binding protein from rat brain: Oligomycin sensitivity-conferring protein (OSCP), a subunit of mitochondrial FOF1-ATP synthase/ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); ESTROGEN BINDING PROTEIN; ESTROGEN RECEPTOR; OLIGOMYCIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 0032997722     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(98)00161-7     Document Type: Article
Times cited : (98)

References (59)
  • 1
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. The steroid and thyroid hormone receptor superfamily. Science. 240:1988;889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 2
    • 0021287331 scopus 로고
    • Lysosomal functions in cellular activation: Propagation of the actions of hormones and other effectors
    • Szego C.M., Pietras R.J. Lysosomal functions in cellular activation: propagation of the actions of hormones and other effectors. Int. Rev. Cytol. 88:1984;1-302.
    • (1984) Int. Rev. Cytol. , vol.88 , pp. 1-302
    • Szego, C.M.1    Pietras, R.J.2
  • 3
    • 0026032108 scopus 로고
    • Nongenomic and genomic effects of steroids on neural activity
    • McEwen B.S. Nongenomic and genomic effects of steroids on neural activity. Trends Pharmacol. Sci. 12:1991;141-147.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 141-147
    • McEwen, B.S.1
  • 4
    • 0030272394 scopus 로고    scopus 로고
    • Membrane sex-steroid receptors in the brain
    • Ramirez V.D., Zheng J. Membrane sex-steroid receptors in the brain. Frontiers Neuroendocrinol. 17:1996;402-439.
    • (1996) Frontiers Neuroendocrinol. , vol.17 , pp. 402-439
    • Ramirez, V.D.1    Zheng, J.2
  • 5
    • 0030633005 scopus 로고    scopus 로고
    • Estrogen: Nontranscriptional signaling pathway
    • Moss R.L., Gu Q., Wong M. Estrogen: nontranscriptional signaling pathway. Rec. Progress Hormone Res. 52:1997;33-69.
    • (1997) Rec. Progress Hormone Res. , vol.52 , pp. 33-69
    • Moss, R.L.1    Gu, Q.2    Wong, M.3
  • 6
    • 0030135415 scopus 로고    scopus 로고
    • Steroids conjugated to bovine serum albumin as tools to demonstrate specific steroid neuronal membrane binding sites
    • Zheng J., Ali A., Ramirez V.D. Steroids conjugated to bovine serum albumin as tools to demonstrate specific steroid neuronal membrane binding sites. J. Psychiat. Neurosci. 21:1996;187-197.
    • (1996) J. Psychiat. Neurosci. , vol.21 , pp. 187-197
    • Zheng, J.1    Ali, A.2    Ramirez, V.D.3
  • 7
    • 0029890498 scopus 로고    scopus 로고
    • Membrane receptors for estrogen, progesterone and testosterone in the rat brain: Fantasy or reality
    • Ramirez V.D., Zheng J., Siddique K.M. Membrane receptors for estrogen, progesterone and testosterone in the rat brain: fantasy or reality. Cell. Mol. Neurobiol. 16:1996;175-198.
    • (1996) Cell. Mol. Neurobiol. , vol.16 , pp. 175-198
    • Ramirez, V.D.1    Zheng, J.2    Siddique, K.M.3
  • 10
    • 0021365236 scopus 로고
    • Validity of a histochemical estrogen receptor assay: Supported by the observation of a cellular response to steroid manipulation
    • Lee S.H. Validity of a histochemical estrogen receptor assay: supported by the observation of a cellular response to steroid manipulation. J. Histochem. Cytochem. 32:1984;305-310.
    • (1984) J. Histochem. Cytochem. , vol.32 , pp. 305-310
    • Lee, S.H.1
  • 14
    • 0027485793 scopus 로고
    • Cell signaling and estrogens in female rat osteoblasts: A possible involvement of unconventional nonnuclear receptors
    • Lieberherr M., Grosse B., Kachkache M., Balsan S. Cell signaling and estrogens in female rat osteoblasts: a possible involvement of unconventional nonnuclear receptors. J. Bone Mineral Res. 8:1993;1365-1376.
    • (1993) J. Bone Mineral Res. , vol.8 , pp. 1365-1376
    • Lieberherr, M.1    Grosse, B.2    Kachkache, M.3    Balsan, S.4
  • 15
    • 0030026862 scopus 로고    scopus 로고
    • Estradiol reduces calcium currents in rat neostriatal neurons via a membrane receptor
    • Mermelstein P.G., Becker J.B., Surmeier D.J. Estradiol reduces calcium currents in rat neostriatal neurons via a membrane receptor. J. Neurosci. 16:1996;595-604.
    • (1996) J. Neurosci. , vol.16 , pp. 595-604
    • Mermelstein, P.G.1    Becker, J.B.2    Surmeier, D.J.3
  • 16
    • 0019867504 scopus 로고
    • Affinity cytochemistry visualizes specific estrogen binding sites on the plasma membrane of breast cancer cells
    • Nenci T., Marchetti E., Marzola A., Fabris G. Affinity cytochemistry visualizes specific estrogen binding sites on the plasma membrane of breast cancer cells. J. Steroid Biochem. 14:1981;1139-1146.
    • (1981) J. Steroid Biochem. , vol.14 , pp. 1139-1146
    • Nenci, T.1    Marchetti, E.2    Marzola, A.3    Fabris, G.4
  • 17
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas T.C., Gametchu B., Watson C.S. Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J. 9:1995;404-410.
    • (1995) FASEB J. , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 18
    • 0025068789 scopus 로고
    • Binding of progesterone to nerve cell membranes of rat brain using progesterone conjugated to I125-bovine serum albumin as a ligand
    • Ke F.C., Ramirez V.D. Binding of progesterone to nerve cell membranes of rat brain using progesterone conjugated to I125-bovine serum albumin as a ligand. J. Neurochem. 54:1990;467-472.
    • (1990) J. Neurochem. , vol.54 , pp. 467-472
    • Ke, F.C.1    Ramirez, V.D.2
  • 19
    • 0024574988 scopus 로고
    • Kainyl-bovine serum albumin: A novel ligand of the kainate subtype of glutamate receptor with a very high binding affinity
    • Eshhar N., Lederkremer G., Beaujean M., Goldberg O., Gregor P., Ortega A., Triller A., Teichberg V.I. Kainyl-bovine serum albumin: a novel ligand of the kainate subtype of glutamate receptor with a very high binding affinity. Brain Res. 476:1989;57-70.
    • (1989) Brain Res. , vol.476 , pp. 57-70
    • Eshhar, N.1    Lederkremer, G.2    Beaujean, M.3    Goldberg, O.4    Gregor, P.5    Ortega, A.6    Triller, A.7    Teichberg, V.I.8
  • 20
    • 0026680290 scopus 로고
    • Oligomycin sensitivity-conferring protein (OSCP) of mitochondrial ATP synthase
    • Joshi S., Javed A.A., Gibbs L.C. Oligomycin sensitivity-conferring protein (OSCP) of mitochondrial ATP synthase. J. Biol. Chem. 267:1992;12860-12867.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12860-12867
    • Joshi, S.1    Javed, A.A.2    Gibbs, L.C.3
  • 21
    • 0020562171 scopus 로고
    • A rapid filtration assay for soluble receptors using polyethylenimine-treated filters
    • Bruns R.F., Lawson-Wendling K., Pugsley T.A. A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal. Biochem. 132:1983;74-81.
    • (1983) Anal. Biochem. , vol.132 , pp. 74-81
    • Bruns, R.F.1    Lawson-Wendling, K.2    Pugsley, T.A.3
  • 22
    • 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
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 261:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.261 , pp. 10035-10038
    • Matsudaira, P.1
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets
    • Towbin H., Staehelin R., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, R.2    Gordon, J.3
  • 26
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson P.J., Rodbard D. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107:1980;220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 28
    • 0022433997 scopus 로고
    • Interactions between the oligomycin sensitivity conferring protein (OSCP) and beef heart mitochondrial F1-ATPase. 1. Study of the binding parameters with a chemically radiolabeled OSCP
    • Dupuis A., Issartel J.-P., Lunardi J., Satre M., Vignais P.V. Interactions between the oligomycin sensitivity conferring protein (OSCP) and beef heart mitochondrial F1-ATPase. 1. Study of the binding parameters with a chemically radiolabeled OSCP. Biochemistry. 24:1985;728-733.
    • (1985) Biochemistry , vol.24 , pp. 728-733
    • Dupuis, A.1    Issartel, J.-P.2    Lunardi, J.3    Satre, M.4    Vignais, P.V.5
  • 29
    • 0345601805 scopus 로고
    • Binding properties and ligand specificity of an intracellular binding site with specificity for synthetic oestrogen antagonists of the triphenylethylene series
    • M.K. Agarwal. Berlin: Walter de Gruyter & Co
    • Sutherland R.L., Watts C.K.W., Murphy L.C. Binding properties and ligand specificity of an intracellular binding site with specificity for synthetic oestrogen antagonists of the triphenylethylene series. Agarwal M.K. Hormone Antagonists. 1982;147-161 Walter de Gruyter & Co, Berlin.
    • (1982) Hormone Antagonists , pp. 147-161
    • Sutherland, R.L.1    Watts, C.K.W.2    Murphy, L.C.3
  • 30
    • 0014465905 scopus 로고
    • Comparative binding affinity of estrogens and its relation to estrogenic potency
    • Korenman S.G. Comparative binding affinity of estrogens and its relation to estrogenic potency. Steroids. 13:1969;163-177.
    • (1969) Steroids , vol.13 , pp. 163-177
    • Korenman, S.G.1
  • 31
    • 0015821567 scopus 로고
    • Affinity chromatography and the purification of estrogen receptors
    • Sica V., Parikh I., Nola E., Puca G.A., Cuatrecasas P. Affinity chromatography and the purification of estrogen receptors. J. Biol. Chem. 248:1973;6543-6558.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6543-6558
    • Sica, V.1    Parikh, I.2    Nola, E.3    Puca, G.A.4    Cuatrecasas, P.5
  • 32
    • 0025806876 scopus 로고
    • Identification of F0 subunits in the rat liver mitochondrial F0F1-ATP synthase
    • Cretin F., Baggetto L.G., Denoroy L., Godinot C. Identification of F0 subunits in the rat liver mitochondrial F0F1-ATP synthase. Biochim. Biophys. Acta. 1058:1991;141-146.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 141-146
    • Cretin, F.1    Baggetto, L.G.2    Denoroy, L.3    Godinot, C.4
  • 34
    • 0027465438 scopus 로고
    • Cardiac nonmyofibrillar proteins in copper-deficient rats: Amino acid sequencing and Western blotting of altered proteins
    • Medeiros D.M., Whiry L., Lincoln A.J., Prochaska L.J. Cardiac nonmyofibrillar proteins in copper-deficient rats: amino acid sequencing and Western blotting of altered proteins. Biol. Trace Element Res. 36:1993;271-282.
    • (1993) Biol. Trace Element Res. , vol.36 , pp. 271-282
    • Medeiros, D.M.1    Whiry, L.2    Lincoln, A.J.3    Prochaska, L.J.4
  • 35
    • 0028921672 scopus 로고
    • ATP synthase complex-proximities of subunits in bovine submitochondrial particles
    • Belogrudov G.I., Tomich J.M., Hatefi Y. ATP synthase complex-proximities of subunits in bovine submitochondrial particles. J. Biol. Chem. 270:1995;2053-2060.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2053-2060
    • Belogrudov, G.I.1    Tomich, J.M.2    Hatefi, Y.3
  • 36
    • 0025924053 scopus 로고
    • The F0 subunits of bovine mitochondrial ATP synthase complex: Purification, antibody production and interspecies cross-immunoreactivity
    • Hekman C., Hatefi Y. The F0 subunits of bovine mitochondrial ATP synthase complex: purification, antibody production and interspecies cross-immunoreactivity. Arch. Biochem. Biophys. 284:1991;90-97.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 90-97
    • Hekman, C.1    Hatefi, Y.2
  • 37
    • 0022901552 scopus 로고
    • Steroid-bovine serum albumin conjugates: Molecular characterization and their interaction with androgen and estrogen receptors
    • De Goeij A.F.P.M., van Zeeland J.K., Beek C.J.L., Bosman F.T. Steroid-bovine serum albumin conjugates: molecular characterization and their interaction with androgen and estrogen receptors. J. Steroid Biochem. 24:1986;1017-1031.
    • (1986) J. Steroid Biochem. , vol.24 , pp. 1017-1031
    • De Goeij, A.F.P.M.1    Van Zeeland, J.K.2    Beek, C.J.L.3    Bosman, F.T.4
  • 39
    • 0028301141 scopus 로고
    • The role of the stalk in the coupling mechanism of F1F0-ATPases
    • Walker J.E., Collinson I.R. The role of the stalk in the coupling mechanism of F1F0-ATPases. FEBS Lett. 346:1994;39-43.
    • (1994) FEBS Lett. , vol.346 , pp. 39-43
    • Walker, J.E.1    Collinson, I.R.2
  • 40
    • 0025139058 scopus 로고
    • +-ATPase: At the interface between proton flow and ATP synthesis
    • +-ATPase: at the interface between proton flow and ATP synthesis. Biochim. Biophys. Acta. 1015:1990;379-390.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 379-390
    • Engelbrecht, S.1    Junge, W.2
  • 41
    • 0021769168 scopus 로고
    • Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the delta-subunit of the F1-ATPase of Escherichia coli
    • Ovchinnikov Y.A., Modyanov N.N., Grinkevich V.A., Aldanova N.A., Trubetskaya O.E., Nazimov I.V., Hundal T., Ernster L. Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the delta-subunit of the F1-ATPase of Escherichia coli. FEBS Lett. 166:1984;19-22.
    • (1984) FEBS Lett. , vol.166 , pp. 19-22
    • Ovchinnikov, Y.A.1    Modyanov, N.N.2    Grinkevich, V.A.3    Aldanova, N.A.4    Trubetskaya, O.E.5    Nazimov, I.V.6    Hundal, T.7    Ernster, L.8
  • 42
    • 0023621390 scopus 로고
    • ATP synthase from bovine mitochondria: Sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6 and adenosinetriphosphatase inhibitor protein
    • Walker J.E., Gay N.J., Powell S.J., Kostina M., Dyer M.R. ATP synthase from bovine mitochondria: sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6 and adenosinetriphosphatase inhibitor protein. Biochemistry. 26:1987;8613-8619.
    • (1987) Biochemistry , vol.26 , pp. 8613-8619
    • Walker, J.E.1    Gay, N.J.2    Powell, S.J.3    Kostina, M.4    Dyer, M.R.5
  • 43
    • 0029962414 scopus 로고    scopus 로고
    • The vascular protective effects of estrogen
    • Farhat M.Y., Lavigne M.C., Ramwell P.W. The vascular protective effects of estrogen. FASEB J. 10:1996;615-624.
    • (1996) FASEB J. , vol.10 , pp. 615-624
    • Farhat, M.Y.1    Lavigne, M.C.2    Ramwell, P.W.3
  • 44
    • 0028971169 scopus 로고
    • 17β-estradiol protects neurons from oxidative stress-induced cell death in vitro
    • Behl C., Widmann M., Trapp T., Holsboer F. 17β-estradiol protects neurons from oxidative stress-induced cell death in vitro. Biochem. Biophys. Res. Commun. 216:1995;473-482.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 473-482
    • Behl, C.1    Widmann, M.2    Trapp, T.3    Holsboer, F.4
  • 45
    • 0030006741 scopus 로고    scopus 로고
    • Inhibition of lipid peroxidation by estradiol and 2-hydroxyestradiol
    • Miura T., Muraoka S., Ogiso T. Inhibition of lipid peroxidation by estradiol and 2-hydroxyestradiol. Steroids. 61:1996;379-383.
    • (1996) Steroids , vol.61 , pp. 379-383
    • Miura, T.1    Muraoka, S.2    Ogiso, T.3
  • 46
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals and neurodegeneration
    • Beal M.F. Mitochondria, free radicals and neurodegeneration. Curr. Opinion Neurobiol. 6:1996;661-666.
    • (1996) Curr. Opinion Neurobiol. , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 47
    • 0006141522 scopus 로고
    • Some aspects of steroid hormone action
    • Tomkins G.M., Maxwell E.S. Some aspects of steroid hormone action. Ann. Rev. Biochem. 32:1963;677-708.
    • (1963) Ann. Rev. Biochem. , vol.32 , pp. 677-708
    • Tomkins, G.M.1    Maxwell, E.S.2
  • 48
    • 0015344569 scopus 로고
    • Inhibition by diethyl stilbestrol of calcium uptake by human myometrial mitochondria
    • Batra S.C., Bengtsson L.P. Inhibition by diethyl stilbestrol of calcium uptake by human myometrial mitochondria. Eur. J. Pharmacol. 18:1972;281-283.
    • (1972) Eur. J. Pharmacol. , vol.18 , pp. 281-283
    • Batra, S.C.1    Bengtsson, L.P.2
  • 49
    • 0022931532 scopus 로고
    • Diethylstilbestrol F0 'proton channel' of rat liver mitochondria: Rapid purification of a functional complex and a study of its interaction with the unique probe diethylstilbestrol
    • McEnery M.W., Pedersen P.L. Diethylstilbestrol F0 'proton channel' of rat liver mitochondria: rapid purification of a functional complex and a study of its interaction with the unique probe diethylstilbestrol. J. Biol. Chem. 261:1986;1745-1752.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1745-1752
    • McEnery, M.W.1    Pedersen, P.L.2
  • 50
    • 0024474490 scopus 로고
    • F0 'proton channel' of rat liver mitochondria: Rapid purification of a functional complex and a study of its interaction with the unique probe diethylstilbestrol
    • McEnery M.W., Hullihen J., Pedersen P.L. F0 'proton channel' of rat liver mitochondria: rapid purification of a functional complex and a study of its interaction with the unique probe diethylstilbestrol. J. Biol. Chem. 264:1989;12029-12036.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12029-12036
    • McEnery, M.W.1    Hullihen, J.2    Pedersen, P.L.3
  • 53
    • 0014845660 scopus 로고
    • The effects of oestradiol on the acid-soluble nucleotides of rat uterus
    • Oliver J.M., Kellie A.E. The effects of oestradiol on the acid-soluble nucleotides of rat uterus. Biochem. J. 119:1970;187-191.
    • (1970) Biochem. J. , vol.119 , pp. 187-191
    • Oliver, J.M.1    Kellie, A.E.2
  • 56
    • 0029040896 scopus 로고
    • Homology of a bovine allergen and the oligomycin sensitivity-conferring protein of the mitochondrial adenosine triphosphate synthase complex
    • Parkkinen S., Rytkonen M., Pentikainen J., Virtanen T., Mantyjarvi R. Homology of a bovine allergen and the oligomycin sensitivity-conferring protein of the mitochondrial adenosine triphosphate synthase complex. J. Allergy Clin. Immunol. 95:1995;1255-1260.
    • (1995) J. Allergy Clin. Immunol. , vol.95 , pp. 1255-1260
    • Parkkinen, S.1    Rytkonen, M.2    Pentikainen, J.3    Virtanen, T.4    Mantyjarvi, R.5
  • 57
    • 0029063982 scopus 로고
    • Identification of novel genes from stomach cancer cell lines by differential display
    • Salesiotis A.N., Wang C.K., Wang C.D., Burger A., Li H., Seth A. Identification of novel genes from stomach cancer cell lines by differential display. Cancer Lett. 91:1995;47-54.
    • (1995) Cancer Lett. , vol.91 , pp. 47-54
    • Salesiotis, A.N.1    Wang, C.K.2    Wang, C.D.3    Burger, A.4    Li, H.5    Seth, A.6
  • 58
    • 0031041325 scopus 로고    scopus 로고
    • Gene expression of subunit c (P1), subunit c (P2) and oligomycin sensitivity-conferring protein may play a key role in biogenesis of H+-ATP synthase in various rat tissues
    • Sangawa H., Himeda T., Shibata H., Higuti T. Gene expression of subunit c (P1), subunit c (P2) and oligomycin sensitivity-conferring protein may play a key role in biogenesis of H+-ATP synthase in various rat tissues. J. Biol. Chem. 272:1997;6034-6037.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6034-6037
    • Sangawa, H.1    Himeda, T.2    Shibata, H.3    Higuti, T.4
  • 59
    • 0028869597 scopus 로고
    • Human diseases with defects in oxidative phosphorylation 2. F1F0 ATP-synthase defects in Alzheimer disease revealed by blue native polyacrylamide gel electrophoresis
    • Schagger H., Ohm T.G. Human diseases with defects in oxidative phosphorylation 2. F1F0 ATP-synthase defects in Alzheimer disease revealed by blue native polyacrylamide gel electrophoresis. Eur. J. Biochem. 227:1995;916-921.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 916-921
    • Schagger, H.1    Ohm, T.G.2


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