메뉴 건너뛰기




Volumn 28, Issue 3, 2005, Pages 239-272

Redox options in two-dimensional electrophoresis

Author keywords

Alkylation; Cysteine; Cystine; Oxidation; Reduction; Serum; Two dimensional electrophoresis

Indexed keywords

ALPHA GLOBULIN; DODECYL SULFATE SODIUM; IMMUNOGLOBULIN; MERCAPTOETHANOL; OLIGOMER; POLYPEPTIDE; PROTEIN SUBUNIT; TRIBUTYLPHOSPHINE; UREA;

EID: 20044383028     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-005-0175-z     Document Type: Review
Times cited : (24)

References (93)
  • 1
    • 0023724979 scopus 로고
    • Isoelectric focusing of basic proteins: The problem of oxidation of cysteines
    • Altland K, Becher P, Rossmann U, Bjellqvist B (1988) Isoelectric focusing of basic proteins: The problem of oxidation of cysteines. Electrophoresis 9: 474-485
    • (1988) Electrophoresis , vol.9 , pp. 474-485
    • Altland, K.1    Becher, P.2    Rossmann, U.3    Bjellqvist, B.4
  • 2
    • 0017721398 scopus 로고
    • High resolution two-dimensional electrophoresis of human plasma proteins
    • Anderson L, Anderson NG (1977) High resolution two-dimensional electrophoresis of human plasma proteins. Proc Natl Acad Sci USA 74: 5421-5425
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5421-5425
    • Anderson, L.1    Anderson, N.G.2
  • 6
    • 0024418720 scopus 로고
    • Isolation of carboxyl-terminal peptides from proteins by diagonal electrophoresis: Application to the entomocidal toxin from Bacillus thuringiensis
    • Bietlot HP, Carey PR, Pozsgay M, Kaplan H (1989) Isolation of carboxyl-terminal peptides from proteins by diagonal electrophoresis: Application to the entomocidal toxin from Bacillus thuringiensis. Anal Biochem 181: 212-215
    • (1989) Anal Biochem , vol.181 , pp. 212-215
    • Bietlot, H.P.1    Carey, P.R.2    Pozsgay, M.3    Kaplan, H.4
  • 7
    • 0018508750 scopus 로고
    • The development of SS′-polymethylenebis(methanethiosulphonates) as reversible cross-linking reagents for thiol groups and their use to form stable catalytically active cross-linked dimers within glyceraldehyde 3-phosphate dehydrogenase
    • Bloxham DP, Sharma RP (1979) The development of SS′- polymethylenebis(methanethiosulphonates) as reversible cross-linking reagents for thiol groups and their use to form stable catalytically active cross-linked dimers within glyceraldehyde 3-phosphate dehydrogenase. Biochem J 181: 355-366
    • (1979) Biochem J , vol.181 , pp. 355-366
    • Bloxham, D.P.1    Sharma, R.P.2
  • 8
    • 4744363388 scopus 로고    scopus 로고
    • Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis
    • Brennan, JP, Wait R, Begum S, Bell JR, Dunn MJ, Eaton P (2004) Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis. J Biol Chem 279: 41352-41360
    • (2004) J Biol Chem , vol.279 , pp. 41352-41360
    • Brennan, J.P.1    Wait, R.2    Begum, S.3    Bell, J.R.4    Dunn, M.J.5    Eaton, P.6
  • 9
    • 1642305355 scopus 로고    scopus 로고
    • Use of staphylococcal protein A in the analysis of teleost immunoglobulin structural diversity
    • Bromage ES, Ye J, Owens L, Kaattari IM, Kaattari SL (2004) Use of staphylococcal protein A in the analysis of teleost immunoglobulin structural diversity. Development Compar Immunol 28: 803-814
    • (2004) Development Compar Immunol , vol.28 , pp. 803-814
    • Bromage, E.S.1    Ye, J.2    Owens, L.3    Kaattari, I.M.4    Kaattari, S.L.5
  • 10
    • 0013958696 scopus 로고
    • Location of disulfide bridges by diagonal paper electrophoresis
    • Brown JR, Hartley BS (1966) Location of disulfide bridges by diagonal paper electrophoresis. Biochem J 101: 214-228
    • (1966) Biochem J , vol.101 , pp. 214-228
    • Brown, J.R.1    Hartley, B.S.2
  • 11
    • 0028801548 scopus 로고
    • Electrophoretic, chromatographic and immunological studies of human urinary proteins
    • Büeler MR, Wiederkehr F, Vonderschmitt DJ (1995) Electrophoretic, chromatographic and immunological studies of human urinary proteins. Electrophoresis 16: 124-134
    • (1995) Electrophoresis , vol.16 , pp. 124-134
    • Büeler, M.R.1    Wiederkehr, F.2    Vonderschmitt, D.J.3
  • 12
    • 0028340631 scopus 로고
    • RNA polymerase II from wheat germ: A cross-linking study of subunits topography
    • Cervoni L, Ferraro A, Giartosio A, Wang C, Turano C (1994) RNA polymerase II from wheat germ: A cross-linking study of subunits topography. Arch Biochem Biophys 311: 35-41
    • (1994) Arch Biochem Biophys , vol.311 , pp. 35-41
    • Cervoni, L.1    Ferraro, A.2    Giartosio, A.3    Wang, C.4    Turano, C.5
  • 13
    • 0023665205 scopus 로고
    • Biosynthesis of chick type VI collagen: I. Intracellular assembly and molecular structure
    • Colombatti A, Bonaldo P, Ainger K, Bressan GM, Volpin D (1987) Biosynthesis of chick type VI collagen: I. Intracellular assembly and molecular structure. J Biol Chem 262: 14454-14460
    • (1987) J Biol Chem , vol.262 , pp. 14454-14460
    • Colombatti, A.1    Bonaldo, P.2    Ainger, K.3    Bressan, G.M.4    Volpin, D.5
  • 14
    • 0019315695 scopus 로고
    • Counting integral numbers of amino acid residues per polypeptide chain
    • Creighton TE (1980) Counting integral numbers of amino acid residues per polypeptide chain. Nature 284(5755): 487-489
    • (1980) Nature , vol.284 , Issue.5755 , pp. 487-489
    • Creighton, T.E.1
  • 15
    • 0016635249 scopus 로고
    • Reactive half-cystine peptides of the secretory component of human exocrine immunoglobulin A
    • Cunningham-Rundles C, Lamm ME (1975) Reactive half-cystine peptides of the secretory component of human exocrine immunoglobulin A. J Biol Chem 250: 1987-1991
    • (1975) J Biol Chem , vol.250 , pp. 1987-1991
    • Cunningham-Rundles, C.1    Lamm, M.E.2
  • 16
    • 0032924806 scopus 로고    scopus 로고
    • Proteins of rat serum: IV. Time-course of acute phase protein expression and its modulation by indomethacin
    • Eberini I, Miller I, Zancan V, Bolego C, Puglisi L, Gemeiner M, Gianazza E (1999) Proteins of rat serum: IV. Time-course of acute phase protein expression and its modulation by indomethacin. Electrophoresis 20: 846-853
    • (1999) Electrophoresis , vol.20 , pp. 846-853
    • Eberini, I.1    Miller, I.2    Zancan, V.3    Bolego, C.4    Puglisi, L.5    Gemeiner, M.6    Gianazza, E.7
  • 19
    • 0019198386 scopus 로고
    • The electrophoresis of transferrins in urea/polyacrylamide gels
    • Evans RW, Williams J (1980) The electrophoresis of transferrins in urea/polyacrylamide gels. Biochem J 189: 541-546
    • (1980) Biochem J , vol.189 , pp. 541-546
    • Evans, R.W.1    Williams, J.2
  • 21
    • 7744224034 scopus 로고    scopus 로고
    • Fully automated online multi-dimensional protein profiling system for complex mixtures
    • Fujii K, Nakano T, Hike H, Usui F, Bando Y, Tojo H, Nishimura T (2004) Fully automated online multi-dimensional protein profiling system for complex mixtures. J Chromatogr A 1057: 107-113
    • (2004) J Chromatogr A , vol.1057 , pp. 107-113
    • Fujii, K.1    Nakano, T.2    Hike, H.3    Usui, F.4    Bando, Y.5    Tojo, H.6    Nishimura, T.7
  • 22
    • 0020649038 scopus 로고
    • Isolation of sulfhydryl peptides alkylated with N-ethylmaleimide by diagonal electrophoresis
    • Gehring H, Christen P (1983) Isolation of sulfhydryl peptides alkylated with N-ethylmaleimide by diagonal electrophoresis. Methods Enzymol 991: 392-396
    • (1983) Methods Enzymol , vol.991 , pp. 392-396
    • Gehring, H.1    Christen, P.2
  • 23
    • 0027730367 scopus 로고
    • Electrophoretic artefacts arising from the use of thiol-containing reagents
    • Gianazza E, De Ponti P (1993) Electrophoretic artefacts arising from the use of thiol-containing reagents. Electrophoresis 14: 1259-1265
    • (1993) Electrophoresis , vol.14 , pp. 1259-1265
    • Gianazza, E.1    De Ponti, P.2
  • 24
    • 0021874579 scopus 로고
    • An improved protocol for 2D maps of serum proteins with immobilized pH gradients in the first dimension
    • Gianazza E, Astrua-Testori S, Giacon P, Righetti PG (1985) An improved protocol for 2D maps of serum proteins with immobilized pH gradients in the first dimension. Electrophoresis 6: 332-339
    • (1985) Electrophoresis , vol.6 , pp. 332-339
    • Gianazza, E.1    Astrua-Testori, S.2    Giacon, P.3    Righetti, P.G.4
  • 27
    • 0032125846 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liver-wort), which contains reaction center and antenna proteins
    • Harrer R, Bassi R, Testi MG, Schafer C (1998) Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liver-wort), which contains reaction center and antenna proteins. Eur J Biochem 255: 196-205
    • (1998) Eur J Biochem , vol.255 , pp. 196-205
    • Harrer, R.1    Bassi, R.2    Testi, M.G.3    Schafer, C.4
  • 28
    • 0025239701 scopus 로고
    • The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: Use of site-specific mutagenesis and recombinant protein expression
    • Hatzfeld M, Weber K (1990) The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: Use of site-specific mutagenesis and recombinant protein expression. J Cell Biol 110: 1199-1210
    • (1990) J Cell Biol , vol.110 , pp. 1199-1210
    • Hatzfeld, M.1    Weber, K.2
  • 29
    • 0031807041 scopus 로고    scopus 로고
    • Proteins of rat serum: I. Establishing a reference 2-DE map by immunodetection and microbore high performance liquid chromatography - Electrospray mass spectrometry
    • Haynes P, Miller I, Aebersold R, Gemeiner M, Eberini I, Lovati MR, Manzoni C, Vignati M, Gianazza E (1998) Proteins of rat serum: I. Establishing a reference 2-DE map by immunodetection and microbore high performance liquid chromatography - electrospray mass spectrometry. Electrophoresis 19: 1484-1492
    • (1998) Electrophoresis , vol.19 , pp. 1484-1492
    • Haynes, P.1    Miller, I.2    Aebersold, R.3    Gemeiner, M.4    Eberini, I.5    Lovati, M.R.6    Manzoni, C.7    Vignati, M.8    Gianazza, E.9
  • 32
    • 0033849340 scopus 로고    scopus 로고
    • Identification of peanut and hazelnut allergens by native two-dimensional gel electrophoresis
    • Hird H, Pumphrey R, Wilson P, Sunderland J, Reece P (2000) Identification of peanut and hazelnut allergens by native two-dimensional gel electrophoresis. Electrophoresis 21: 2678-2683
    • (2000) Electrophoresis , vol.21 , pp. 2678-2683
    • Hird, H.1    Pumphrey, R.2    Wilson, P.3    Sunderland, J.4    Reece, P.5
  • 34
    • 0022730455 scopus 로고
    • A class of cleavable heterobifunctional reagents for thiol-directed high-efficiency protein crosslinking: Synthesis and application to the analysis of protein contact sites in mammalian ribosomes
    • Hultin T (1986) A class of cleavable heterobifunctional reagents for thiol-directed high-efficiency protein crosslinking: Synthesis and application to the analysis of protein contact sites in mammalian ribosomes. Anal Biochem 155: 262-269
    • (1986) Anal Biochem , vol.155 , pp. 262-269
    • Hultin, T.1
  • 35
    • 0022533186 scopus 로고
    • Selective high-efficiency cross-linking of mammalian ribosomal proteins with cleavable thiol-directed heterobifunctional reagents: Separation and identification of contact sequences of neighboring proteins after CNBr fragmentation
    • Hultin T, Nika H (1986) Selective high-efficiency cross-linking of mammalian ribosomal proteins with cleavable thiol-directed heterobifunctional reagents: Separation and identification of contact sequences of neighboring proteins after CNBr fragmentation. Biochim Biophys Acta 872: 236-242
    • (1986) Biochim Biophys Acta , vol.872 , pp. 236-242
    • Hultin, T.1    Nika, H.2
  • 36
    • 0001665613 scopus 로고
    • Abnormal human hemoglobins. III. The chemical difference between normal and sickle cell haemoglobins
    • Ingram VM (1959) Abnormal human hemoglobins. III. The chemical difference between normal and sickle cell haemoglobins. Biochim Biophys Acta 26: 402-411
    • (1959) Biochim Biophys Acta , vol.26 , pp. 402-411
    • Ingram, V.M.1
  • 37
    • 0030250383 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of higher-plant photosystem I holocomplex
    • Jansson S, Andersen B, Scheller HV (1996) Nearest-neighbor analysis of higher-plant photosystem I holocomplex. Plant Physiol 112: 409-420
    • (1996) Plant Physiol , vol.112 , pp. 409-420
    • Jansson, S.1    Andersen, B.2    Scheller, H.V.3
  • 38
    • 9144272333 scopus 로고    scopus 로고
    • Diminished synthesis of subunit α (ATP6) and altered function of ATP synthase and cytochrome c oxidase due to the mtDNA 2 bp microdeletion of TA at positions 9205 and 9206
    • Jesina P, Tesarova M, Fornuskova D, Vojtiskova A, Pecina P, Kaplanova V, Hansikova H, Zeman J, Houstek J (2004) Diminished synthesis of subunit α (ATP6) and altered function of ATP synthase and cytochrome c oxidase due to the mtDNA 2 bp microdeletion of TA at positions 9205 and 9206. Biochem J 383: 561-571
    • (2004) Biochem J , vol.383 , pp. 561-571
    • Jesina, P.1    Tesarova, M.2    Fornuskova, D.3    Vojtiskova, A.4    Pecina, P.5    Kaplanova, V.6    Hansikova, H.7    Zeman, J.8    Houstek, J.9
  • 39
    • 0023871074 scopus 로고
    • Characterization of disulfide-linked crystallins associated with human cataractous lens membranes
    • Kodama T, Takemoto L (1988) Characterization of disulfide-linked crystallins associated with human cataractous lens membranes. Investig Ophthalmol Vis Sci 29: 145-149
    • (1988) Investig Ophthalmol Vis Sci , vol.29 , pp. 145-149
    • Kodama, T.1    Takemoto, L.2
  • 40
    • 0025831940 scopus 로고
    • A practicable two-dimensional electrophoresis of urinary proteins as a useful tool in medical diagnosis
    • Lapin A, Feigl W (1991) A practicable two-dimensional electrophoresis of urinary proteins as a useful tool in medical diagnosis. Electrophoresis 12: 472-478
    • (1991) Electrophoresis , vol.12 , pp. 472-478
    • Lapin, A.1    Feigl, W.2
  • 41
    • 0018803826 scopus 로고
    • Structure of potato carboxypeptidase inhibitor: Disulfide pairing and exposure of aromatic residues
    • Leary TR, Grahn DT, Neurath H, Hass GM (1979) Structure of potato carboxypeptidase inhibitor: Disulfide pairing and exposure of aromatic residues. Biochemistry 18: 2252-2256
    • (1979) Biochemistry , vol.18 , pp. 2252-2256
    • Leary, T.R.1    Grahn, D.T.2    Neurath, H.3    Hass, G.M.4
  • 42
    • 0018411624 scopus 로고
    • Two-dimensional electrophoresis of plasma proteins without denaturing agents
    • Tokyo
    • Manabe T, Tachi K, Kojima K, Okuyama T (1979) Two-dimensional electrophoresis of plasma proteins without denaturing agents. J Biochem (Tokyo) 85(3): 649-659
    • (1979) J Biochem , vol.85 , Issue.3 , pp. 649-659
    • Manabe, T.1    Tachi, K.2    Kojima, K.3    Okuyama, T.4
  • 43
    • 0019223692 scopus 로고
    • Two-dimensional electrophoresis of immunoglobulin myeloma proteins in the absence of denaturing agents
    • Tokyo
    • Manabe T, Takahashi N, Kojima K, Shinoda T, Okuyama T (1980) Two-dimensional electrophoresis of immunoglobulin myeloma proteins in the absence of denaturing agents. J Biochem (Tokyo) 87(2): 451-464
    • (1980) J Biochem , vol.87 , Issue.2 , pp. 451-464
    • Manabe, T.1    Takahashi, N.2    Kojima, K.3    Shinoda, T.4    Okuyama, T.5
  • 44
    • 0019821393 scopus 로고
    • Detection of the changes in protein distribution of rat plasma induced by carbon tetrachloride administration by means of two-dimensional electrophoresis
    • Manabe T, Okuyama T, Suzuki A, Shigematsu A (1981) Detection of the changes in protein distribution of rat plasma induced by carbon tetrachloride administration by means of two-dimensional electrophoresis. J Chromatogr 225(1): 65-71
    • (1981) J Chromatogr , vol.225 , Issue.1 , pp. 65-71
    • Manabe, T.1    Okuyama, T.2    Suzuki, A.3    Shigematsu, A.4
  • 45
    • 0020056713 scopus 로고
    • Microscale multisample two-dimensional electrophoresis of proteins in human serum, cerebrospinal fluid, and urine
    • Manabe T, Hayama E, Okuyama T (1982a) Microscale multisample two-dimensional electrophoresis of proteins in human serum, cerebrospinal fluid, and urine. Clin Chem 28: 824-827
    • (1982) Clin Chem , vol.28 , pp. 824-827
    • Manabe, T.1    Hayama, E.2    Okuyama, T.3
  • 46
    • 0020108343 scopus 로고
    • Separation of extremely acidic proteins, S-100 proteins and calmodulin, in some bovine tissues and mammalian brains by two-dimensional electrophoresis in the absence of denaturing agents
    • Tokyo
    • Manabe T, Jitzukawa S, Ishioka N, Isobe T, Okuyama T (1982b) Separation of extremely acidic proteins, S-100 proteins and calmodulin, in some bovine tissues and mammalian brains by two-dimensional electrophoresis in the absence of denaturing agents. J Biochem (Tokyo) 91(3): 1009-1015
    • (1982) J Biochem , vol.91 , Issue.3 , pp. 1009-1015
    • Manabe, T.1    Jitzukawa, S.2    Ishioka, N.3    Isobe, T.4    Okuyama, T.5
  • 47
    • 84988074684 scopus 로고
    • Identification of bovine fetal and adult serum/plasma proteins by two-dimensional electrophoresis and immunochemical staining
    • Manabe T, Takahashi Y, Okuyama T (1987a) Identification of bovine fetal and adult serum/plasma proteins by two-dimensional electrophoresis and immunochemical staining. Electrophoresis 8: 573-578
    • (1987) Electrophoresis , vol.8 , pp. 573-578
    • Manabe, T.1    Takahashi, Y.2    Okuyama, T.3
  • 48
    • 0023280962 scopus 로고
    • Evaluation of lipoproteins and apolipoproteins in serum of a Tangier patient by microscale two-dimensional electrophoresis
    • Manabe T, Visvikis S, Dumon MF, Clerc M, Siest G (1987b) Evaluation of lipoproteins and apolipoproteins in serum of a Tangier patient by microscale two-dimensional electrophoresis. Clin Chem 33(4): 468-472
    • (1987) Clin Chem , vol.33 , Issue.4 , pp. 468-472
    • Manabe, T.1    Visvikis, S.2    Dumon, M.F.3    Clerc, M.4    Siest, G.5
  • 49
    • 0032900441 scopus 로고    scopus 로고
    • A nondenaturing protein map of human plasma proteins correlated with a denaturing polypeptide map combining techniques of micro two-dimensional gel electrophoresis
    • Manabe T, Mizuma H, Watanabe K (1999) A nondenaturing protein map of human plasma proteins correlated with a denaturing polypeptide map combining techniques of micro two-dimensional gel electrophoresis. Electrophoresis 20(4-5): 830-835
    • (1999) Electrophoresis , vol.20 , Issue.4-5 , pp. 830-835
    • Manabe, T.1    Mizuma, H.2    Watanabe, K.3
  • 50
    • 0038385494 scopus 로고    scopus 로고
    • Detection of protein-protein interactions and a group of immunoglobulin G-associated minor proteins in human plasma by nondenaturing and denaturing two-dimensional gel electrophoresis
    • Manabe T, Yamaguchi N, Mukai J, Hamada O, Tani O (2003) Detection of protein-protein interactions and a group of immunoglobulin G-associated minor proteins in human plasma by nondenaturing and denaturing two-dimensional gel electrophoresis. Proteomics 3(6): 832-846
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 832-846
    • Manabe, T.1    Yamaguchi, N.2    Mukai, J.3    Hamada, O.4    Tani, O.5
  • 51
    • 0025833259 scopus 로고
    • The simplified technique of high resolution two-dimensional polyacrylamide gel electrophoresis: Biomedical applications in health and disease
    • Marshall T, Williams KM (1991) The simplified technique of high resolution two-dimensional polyacrylamide gel electrophoresis: Biomedical applications in health and disease. Electrophoresis 12: 461-471
    • (1991) Electrophoresis , vol.12 , pp. 461-471
    • Marshall, T.1    Williams, K.M.2
  • 52
    • 0033035886 scopus 로고    scopus 로고
    • Electrophoretic analysis of Bence Jones proteinuria
    • Marshall T, Williams KM (1999) Electrophoretic analysis of Bence Jones proteinuria. Electrophoresis 20: 1307-1324
    • (1999) Electrophoresis , vol.20 , pp. 1307-1324
    • Marshall, T.1    Williams, K.M.2
  • 53
    • 0005008505 scopus 로고
    • Haptoglobintypisierung von Serumproben ausgewählter Säugetiere mittels Stärkegelelektrophorese
    • Meier F, Seidel B, Geserick G, Luther P, Patzelt D (1980) Haptoglobintypisierung von Serumproben ausgewählter Säugetiere mittels Stärkegelelektrophorese. Mh Vet-Med 35: 617-620
    • (1980) Mh Vet-Med , vol.35 , pp. 617-620
    • Meier, F.1    Seidel, B.2    Geserick, G.3    Luther, P.4    Patzelt, D.5
  • 54
    • 0032059165 scopus 로고    scopus 로고
    • High preβ1-HDL levels in hypercholesterolemia are maintained by probucol but reduced by a low-cholesterol diet
    • Miida T, Yamaguchi T, Tsuda T, Okada M (1998) High preβ1-HDL levels in hypercholesterolemia are maintained by probucol but reduced by a low-cholesterol diet. Atherosclerosis 138: 129-134
    • (1998) Atherosclerosis , vol.138 , pp. 129-134
    • Miida, T.1    Yamaguchi, T.2    Tsuda, T.3    Okada, M.4
  • 55
    • 0033621751 scopus 로고    scopus 로고
    • Preβ1-high-density lipoprotein (prebeta1-HDL) concentration can change with low-density lipoprotein-cholesterol (LDL-C) concentration independent of cholesteryl ester transfer protein (CETP)
    • Miida T, Ozaki K, Murakami T, Kashiwa T, Yamadera T, Tsuda T, Inano K, Okada M (2000) Preβ1-high-density lipoprotein (prebeta1-HDL) concentration can change with low-density lipoprotein-cholesterol (LDL-C) concentration independent of cholesteryl ester transfer protein (CETP). Clin Chim Acta 292: 69-80
    • (2000) Clin Chim Acta , vol.292 , pp. 69-80
    • Miida, T.1    Ozaki, K.2    Murakami, T.3    Kashiwa, T.4    Yamadera, T.5    Tsuda, T.6    Inano, K.7    Okada, M.8
  • 58
    • 85145635688 scopus 로고    scopus 로고
    • Immunoglobulin patterns in health and disease
    • Lazarev A, Smejkal G (eds) CRC (in press)
    • Miller I, Goldfarb M (2005) Immunoglobulin patterns in health and disease. In: Lazarev A, Smejkal G (eds) Separation methods in proteomics. CRC (in press)
    • (2005) Separation Methods in Proteomics
    • Miller, I.1    Goldfarb, M.2
  • 60
    • 0032955617 scopus 로고    scopus 로고
    • Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation
    • Miller I, Haynes P, Eberini I, Gemeiner M, Aebersold R, Gianazza E (1999) Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation. Electrophoresis 20: 836-845
    • (1999) Electrophoresis , vol.20 , pp. 836-845
    • Miller, I.1    Haynes, P.2    Eberini, I.3    Gemeiner, M.4    Aebersold, R.5    Gianazza, E.6
  • 61
    • 0942276232 scopus 로고    scopus 로고
    • Nonreducing two-dimensional gel electrophoresis for the detection of Bence Jones proteins in serum and urine
    • Miller I, Teinfalt M, Leschnik M, Wait R, Gemeiner M (2004) Nonreducing two-dimensional gel electrophoresis for the detection of Bence Jones proteins in serum and urine. Proteomics 4: 257-260
    • (2004) Proteomics , vol.4 , pp. 257-260
    • Miller, I.1    Teinfalt, M.2    Leschnik, M.3    Wait, R.4    Gemeiner, M.5
  • 62
    • 0014197126 scopus 로고
    • Selective purification of phosphoserine peptides by diagonal electrophoresis
    • Milstein CP (1967) Selective purification of phosphoserine peptides by diagonal electrophoresis. Nature 215: 1190-1191
    • (1967) Nature , vol.215 , pp. 1190-1191
    • Milstein, C.P.1
  • 64
    • 0024558647 scopus 로고
    • Improved separation of α chains of collagen type I, type III, and type V by noninterrupted electrophoresis using thioglycolic acid as a negatively charged reducer
    • Nakamura K, Inoue S, Abiko S, Aoki H, Takeo K (1989) Improved separation of α chains of collagen type I, type III, and type V by noninterrupted electrophoresis using thioglycolic acid as a negatively charged reducer. Electrophoresis 10: 29-33
    • (1989) Electrophoresis , vol.10 , pp. 29-33
    • Nakamura, K.1    Inoue, S.2    Abiko, S.3    Aoki, H.4    Takeo, K.5
  • 65
    • 0036858458 scopus 로고    scopus 로고
    • Organic disulfides as a means to generate streak-free two-dimensional maps with narrow range basic immobilized pH gradient strips as first dimension
    • Olsson I, Larsson K, Palmgren R, Bjellqvist B (2002) Organic disulfides as a means to generate streak-free two-dimensional maps with narrow range basic immobilized pH gradient strips as first dimension. Proteomics 2: 1630-1632
    • (2002) Proteomics , vol.2 , pp. 1630-1632
    • Olsson, I.1    Larsson, K.2    Palmgren, R.3    Bjellqvist, B.4
  • 66
    • 0016634447 scopus 로고
    • Identification of functional arginine residues in ribonuclease A and lysozyme
    • Patthy L, Smith EL (1975) Identification of functional arginine residues in ribonuclease A and lysozyme. J Biol Chem 250: 565-569
    • (1975) J Biol Chem , vol.250 , pp. 565-569
    • Patthy, L.1    Smith, E.L.2
  • 67
    • 0020170370 scopus 로고
    • Effect of 2-mercaptoethanol on pH gradients in isoelectric focusing
    • Righetti PG, Tudor G, Gianazza E (1982) Effect of 2-mercaptoethanol on pH gradients in isoelectric focusing. J Biochem Biophys Methods 6: 219-227
    • (1982) J Biochem Biophys Methods , vol.6 , pp. 219-227
    • Righetti, P.G.1    Tudor, G.2    Gianazza, E.3
  • 68
    • 0017729399 scopus 로고
    • Reductive cleavage of cystine disulfides with tributylphosphine
    • Ruegg UT, Rudinger J (1977) Reductive cleavage of cystine disulfides with tributylphosphine. Methods Enzymol 47: 111-116
    • (1977) Methods Enzymol , vol.47 , pp. 111-116
    • Ruegg, U.T.1    Rudinger, J.2
  • 69
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H, von Jagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199: 223-231
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 70
    • 84988072856 scopus 로고
    • Ultrathin-layer sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis and silver staining of urinary proteins
    • Schiwara H-W, Hebell T, Kirchherr H, Postel W, Weser J, Görg A (1986) Ultrathin-layer sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis and silver staining of urinary proteins. Electrophoresis 7: 496-505
    • (1986) Electrophoresis , vol.7 , pp. 496-505
    • Schiwara, H.-W.1    Hebell, T.2    Kirchherr, H.3    Postel, W.4    Weser, J.5    Görg, A.6
  • 71
    • 0031692675 scopus 로고    scopus 로고
    • Removal of specific protein spots on the patterns of non-denaturing two-dimensional electrophoresis using protein A agarose and antibodies
    • Shimazaki Y, Ohara S, Manabe T (1998) Removal of specific protein spots on the patterns of non-denaturing two-dimensional electrophoresis using protein A agarose and antibodies. J Biochem Biophys Methods 37(1-2): 1-4
    • (1998) J Biochem Biophys Methods , vol.37 , Issue.1-2 , pp. 1-4
    • Shimazaki, Y.1    Ohara, S.2    Manabe, T.3
  • 72
    • 0032947948 scopus 로고    scopus 로고
    • Protein spot recognition on the non-denaturing and denaturing two-dimensional electrophoresis patterns using in situ immunosubtraction via Protein A agarose and antibodies
    • Shimazaki Y, Ohara S, Manabe T (1999) Protein spot recognition on the non-denaturing and denaturing two-dimensional electrophoresis patterns using in situ immunosubtraction via Protein A agarose and antibodies. J Biochem Biophys Methods 39(3): 179-184
    • (1999) J Biochem Biophys Methods , vol.39 , Issue.3 , pp. 179-184
    • Shimazaki, Y.1    Ohara, S.2    Manabe, T.3
  • 73
    • 0033763843 scopus 로고    scopus 로고
    • Selection of an effective enzyme for digestion of non-denaturing proteins using microscale two-dimensional electrophoresis
    • Shimazaki Y, Muro M, Manabe T (2000) Selection of an effective enzyme for digestion of non-denaturing proteins using microscale two-dimensional electrophoresis. Clin Chim Acta 302(1-2): 221-224
    • (2000) Clin Chim Acta , vol.302 , Issue.1-2 , pp. 221-224
    • Shimazaki, Y.1    Muro, M.2    Manabe, T.3
  • 74
    • 0142151382 scopus 로고    scopus 로고
    • Analysis of the activity and identification of enzymes after separation of cytosol proteins in mouse liver by microscale nondenaturing two-dimensional electrophoresis
    • Shimazaki Y, Sugawara Y, Ohtsuka Y, Manabe T (2003) Analysis of the activity and identification of enzymes after separation of cytosol proteins in mouse liver by microscale nondenaturing two-dimensional electrophoresis. Proteomics 3(10): 2002-2007
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 2002-2007
    • Shimazaki, Y.1    Sugawara, Y.2    Ohtsuka, Y.3    Manabe, T.4
  • 75
    • 1242284207 scopus 로고    scopus 로고
    • Simultaneous analysis of esterase and transferase activities in cytosol proteins from the bovine retina by using microscale non-denaturing two-dimensional electrophoresis
    • Shimazaki Y, Hiraka Y, Uesugi M, Manabe T (2004a) Simultaneous analysis of esterase and transferase activities in cytosol proteins from the bovine retina by using microscale non-denaturing two-dimensional electrophoresis. Biochim Biophys Acta 1696(1): 51-57
    • (2004) Biochim Biophys Acta , vol.1696 , Issue.1 , pp. 51-57
    • Shimazaki, Y.1    Hiraka, Y.2    Uesugi, M.3    Manabe, T.4
  • 76
    • 2442499230 scopus 로고    scopus 로고
    • Nondenaturing two-dimensional electrophoresis enzyme profile involving activity and sequence structure of cytosol proteins from mouse liver
    • Shimazaki Y, Sugawara Y, Manabe T (2004b) Nondenaturing two-dimensional electrophoresis enzyme profile involving activity and sequence structure of cytosol proteins from mouse liver. Proteomics 4(5): 1406-1411
    • (2004) Proteomics , vol.4 , Issue.5 , pp. 1406-1411
    • Shimazaki, Y.1    Sugawara, Y.2    Manabe, T.3
  • 77
    • 0022517917 scopus 로고
    • Electrophoretic determination of sulfhydryl groups and its application to complex protein samples, in vitro protein synthesis mixtures, and cross-linked proteins
    • Stan-Lotter H, Bragg PD (1986) Electrophoretic determination of sulfhydryl groups and its application to complex protein samples, in vitro protein synthesis mixtures, and cross-linked proteins. Biochem Cell Biol 64: 154-160
    • (1986) Biochem Cell Biol , vol.64 , pp. 154-160
    • Stan-Lotter, H.1    Bragg, P.D.2
  • 79
    • 0017644458 scopus 로고
    • Analysis of membrane protein topography of Newcastle disease virus and cultured mammalian fibrablasts
    • Takemoto LJ, Miyakawa T, Fox CF (1977) Analysis of membrane protein topography of Newcastle disease virus and cultured mammalian fibrablasts. Progr Clin Biol Res 17: 605-614
    • (1977) Progr Clin Biol Res , vol.17 , pp. 605-614
    • Takemoto, L.J.1    Miyakawa, T.2    Fox, C.F.3
  • 81
    • 0020062170 scopus 로고
    • Two-dimensional gel electrophoresis of serum specimens from patients with monoclonal gammopathies
    • Tracy RP, Currie RM, Kyle RA, Young DS (1982) Two-dimensional gel electrophoresis of serum specimens from patients with monoclonal gammopathies. Clin Chem 28: 900-907
    • (1982) Clin Chem , vol.28 , pp. 900-907
    • Tracy, R.P.1    Currie, R.M.2    Kyle, R.A.3    Young, D.S.4
  • 82
    • 0021744583 scopus 로고
    • Phylogenetical and ontogenetical studies on the molecular weight heterogeneity of bovine serum transferrin
    • Tsuji S, Kato H, Matsuoka Y, Fukushima T, Nanjoh I, Amano T, Namikawa T (1984) Phylogenetical and ontogenetical studies on the molecular weight heterogeneity of bovine serum transferrin. Biochem Genet 22: 1127-1143
    • (1984) Biochem Genet , vol.22 , pp. 1127-1143
    • Tsuji, S.1    Kato, H.2    Matsuoka, Y.3    Fukushima, T.4    Nanjoh, I.5    Amano, T.6    Namikawa, T.7
  • 83
    • 0016649276 scopus 로고
    • Selective separation of tryptophan derivatives using sulfenyl halides
    • Veronese FM, Fontana A, Boccu E (1975) Selective separation of tryptophan derivatives using sulfenyl halides. Acta Vitaminol Enzymol 29: 243-247
    • (1975) Acta Vitaminol Enzymol , vol.29 , pp. 243-247
    • Veronese, F.M.1    Fontana, A.2    Boccu, E.3
  • 84
    • 0023183286 scopus 로고
    • Plasma apolipoproteins in Tangier disease, as studied with two-dimensional electrophoresis
    • Visvikis S, Dumon MF, Steinmetz J, Manabe T, Galteau MM, Clerc M, Siest G (1987) Plasma apolipoproteins in Tangier disease, as studied with two-dimensional electrophoresis. Clin Chem 33(1): 120-122
    • (1987) Clin Chem , vol.33 , Issue.1 , pp. 120-122
    • Visvikis, S.1    Dumon, M.F.2    Steinmetz, J.3    Manabe, T.4    Galteau, M.M.5    Clerc, M.6    Siest, G.7
  • 85
    • 0028962995 scopus 로고
    • Extracellular matrix induces hormone responsiveness and differentiation in RUCA-I rat endometrial adenocarcinoma cells
    • Vollmer G, Ellerbrake N, Hopert AC, Knauthe R, Wunsche W, Knuppen R (1995) Extracellular matrix induces hormone responsiveness and differentiation in RUCA-I rat endometrial adenocarcinoma cells. J Steroid Biochem Mol Biol 52: 259-269
    • (1995) J Steroid Biochem Mol Biol , vol.52 , pp. 259-269
    • Vollmer, G.1    Ellerbrake, N.2    Hopert, A.C.3    Knauthe, R.4    Wunsche, W.5    Knuppen, R.6
  • 87
    • 0034848903 scopus 로고    scopus 로고
    • Proteins of rat serum, urine and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison
    • Wait R, Gianazza E, Eberini I, Sironi L, Dunn MJ, Gemeiner M, Miller I (2001) Proteins of rat serum, urine and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison. Electrophoresis 22: 3043-3052
    • (2001) Electrophoresis , vol.22 , pp. 3043-3052
    • Wait, R.1    Gianazza, E.2    Eberini, I.3    Sironi, L.4    Dunn, M.J.5    Gemeiner, M.6    Miller, I.7
  • 89
    • 0030087534 scopus 로고    scopus 로고
    • Purification and partial molecular characterization of GRP94, an ER resident chaperone
    • Wearsch PA, Nicchitta CV (1996) Purification and partial molecular characterization of GRP94, an ER resident chaperone. Protein Expression Purification 7: 114-121
    • (1996) Protein Expression Purification , vol.7 , pp. 114-121
    • Wearsch, P.A.1    Nicchitta, C.V.2
  • 90
    • 0023748518 scopus 로고
    • Urinary protein analysis
    • Weber MH (1988) Urinary protein analysis. J Chromatogr 429: 315-344
    • (1988) J Chromatogr , vol.429 , pp. 315-344
    • Weber, M.H.1
  • 91
    • 52849103783 scopus 로고    scopus 로고
    • Analysis of the disulfide bonding pattern between domain sequences of recombinant prochymosin solubilized from inclusion bodies
    • Wei C, Chen H, Zhang Y, Yang K (2000) Analysis of the disulfide bonding pattern between domain sequences of recombinant prochymosin solubilized from inclusion bodies. J Prot Chem 19: 277-284
    • (2000) J Prot Chem , vol.19 , pp. 277-284
    • Wei, C.1    Chen, H.2    Zhang, Y.3    Yang, K.4
  • 92
    • 0029588525 scopus 로고
    • Structural and functional characteristics of partially disulfide-reduced intermediates of ovotransferrin N lobe: Cystine localization by indirect end-labeling approach and implications for the reduction pathway
    • Yamashita H, Nakatsuka T, Hirose M (1995) Structural and functional characteristics of partially disulfide-reduced intermediates of ovotransferrin N lobe: Cystine localization by indirect end-labeling approach and implications for the reduction pathway. J Biol Chem 270: 29806-29812
    • (1995) J Biol Chem , vol.270 , pp. 29806-29812
    • Yamashita, H.1    Nakatsuka, T.2    Hirose, M.3
  • 93
    • 0942276401 scopus 로고    scopus 로고
    • Light-harvesting complex II binds to several small subunits of photosystem I
    • Zhang S, Scheller HV (2004) Light-harvesting complex II binds to several small subunits of photosystem I. J Biol Chem 279: 3180-3187
    • (2004) J Biol Chem , vol.279 , pp. 3180-3187
    • Zhang, S.1    Scheller, H.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.