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Volumn 11, Issue 9, 2011, Pages 1834-1839

Low-SDS Blue native PAGE

Author keywords

2 D Blue native SDS PAGE; Blue native PAGE; Destabilization; Plant proteomics; Protein complex; SDS

Indexed keywords

DODECYL SULFATE SODIUM; VEGETABLE PROTEIN;

EID: 79955009768     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000638     Document Type: Article
Times cited : (8)

References (18)
  • 1
    • 0014015432 scopus 로고
    • Disc electrophoresis of proteins in the presence of sodium dodecyl sulphate
    • De Vito, E., Santomé, J. A., Disc electrophoresis of proteins in the presence of sodium dodecyl sulphate. Experientia 1966, 22, 124-125.
    • (1966) Experientia , vol.22 , pp. 124-125
    • De Vito, E.1    Santomé, J.A.2
  • 2
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro, A. L., Viñuela, E., Maizel Jr J. V., Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 1967, 28, 815-820.
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Viñuela, E.2    Maizel Jr, J.V.3
  • 3
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K., Osborn, M., The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 1969, 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 4
    • 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 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 5
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H, von Jagow G., Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 6
    • 50549181757 scopus 로고
    • Two new staining procedures for quantitative estimation of proteins on electrophoretic strips
    • Fazekas de St Groth, S., Webster, R. G., Datyner, A., Two new staining procedures for quantitative estimation of proteins on electrophoretic strips. Biochim. Biophys. Acta 1963, 71, 377-391.
    • (1963) Biochim. Biophys. Acta , vol.71 , pp. 377-391
    • Fazekas de St Groth, S.1    Webster, R.G.2    Datyner, A.3
  • 7
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger, H., Pfeiffer, K., Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 2000, 19, 1777-1783.
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 8
    • 33744901613 scopus 로고    scopus 로고
    • Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
    • Eubel, H., Braun, H. P., Millar, A. H., Blue-native PAGE in plants: a tool in analysis of protein-protein interactions. Plant Methods 2005, 1, 11.
    • (2005) Plant Methods , vol.1 , pp. 11
    • Eubel, H.1    Braun, H.P.2    Millar, A.H.3
  • 9
    • 0036221525 scopus 로고    scopus 로고
    • The cf-9 disease resistance protein is present in an similar to 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex
    • Rivas, S., Romeis, T., Jones, J. D. G., The cf-9 disease resistance protein is present in an similar to 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex. Plant Cell 2002, 14, 689-702.
    • (2002) Plant Cell , vol.14 , pp. 689-702
    • Rivas, S.1    Romeis, T.2    Jones, J.D.G.3
  • 10
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates - a proteomics approach
    • Camacho-Carvajal, M. M., Wollscheid, B., Aebersold, R., Steimle, V., Schamel, W. W. A., Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates - a proteomics approach. Mol. Cell. Proteomics 2004, 3, 176-182.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.A.5
  • 11
    • 77953226426 scopus 로고    scopus 로고
    • Internal architecture of mitochondrial complex I from Arabidopsis thaliana
    • Klodmann, J., Sunderhaus, S., Nimtz, M., Jänsch, L., Braun, H. P., Internal architecture of mitochondrial complex I from Arabidopsis thaliana. Plant Cell 2010, 22, 797-810.
    • (2010) Plant Cell , vol.22 , pp. 797-810
    • Klodmann, J.1    Sunderhaus, S.2    Nimtz, M.3    Jänsch, L.4    Braun, H.P.5
  • 12
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20
    • Werhahn, W., Niemeyer, A., Jänsch, L., Kruft, V. et al., Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20. Plant Physiol. 2001, 125, 943-954.
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4
  • 14
    • 40949142795 scopus 로고    scopus 로고
    • Two-dimensional blue native/blue native polyacrylamide gel electrophoresis for the characterization of mitochondrial protein complexes and supercomplexes
    • Sunderhaus, S., Eubel, H., Braun, H. P., Two-dimensional blue native/blue native polyacrylamide gel electrophoresis for the characterization of mitochondrial protein complexes and supercomplexes. Methods Mol. Biol. 2007, 372, 315-324.
    • (2007) Methods Mol. Biol. , vol.372 , pp. 315-324
    • Sunderhaus, S.1    Eubel, H.2    Braun, H.P.3
  • 15
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., Ehrhardt, W., Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 16
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven, J., Dernick, R., Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 1988, 9, 28-32.
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 17
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel, H., Jänsch, L., Braun, H. P., New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol. 2003, 133, 274-286.
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1    Jänsch, L.2    Braun, H.P.3
  • 18
    • 33845416970 scopus 로고    scopus 로고
    • Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes
    • Shibatani, T., Carlson, E. J., Larabee, F., McCormack, A. L. et al., Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes. Mol. Biol. Cell. 2006, 17, 4962-4971.
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.