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Volumn 112, Issue 1, 2006, Pages 25-27

A rapid method for the recovery, quantification and electrophoretic analysis of proteins from beer

Author keywords

Beer proteins; Electrophoresis; Protein quantification; Protein recovery

Indexed keywords


EID: 33744519149     PISSN: 00469750     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.2050-0416.2006.tb00703.x     Document Type: Article
Times cited : (9)

References (18)
  • 1
    • 0000038821 scopus 로고
    • Characterization of haze-forming proteins of beer and their roles in chill haze formation
    • Asano, K., Shinagawa, K. and Hashimoto, N., Characterization of haze-forming proteins of beer and their roles in chill haze formation. J. Am. Soc. Brew. Chem., 1982, 40, 147-154.
    • (1982) J. Am. Soc. Brew. Chem. , vol.40 , pp. 147-154
    • Asano, K.1    Shinagawa, K.2    Hashimoto, N.3
  • 2
    • 0001686333 scopus 로고
    • Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form
    • Brussels, IRL Press: Oxford
    • Bech, L.M., Vaag, P., Heinemann, B. and Breddam, K., Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form. Proceedings of the European Brewery Convention Congress, Brussels, IRL Press: Oxford, 1995, pp. 561-568.
    • (1995) Proceedings of the European Brewery Convention Congress , pp. 561-568
    • Bech, L.M.1    Vaag, P.2    Heinemann, B.3    Breddam, K.4
  • 3
    • 0028351142 scopus 로고
    • A new two-step precipitation method removes free-SDS and thiol reagents from diluted solutions, and then allows recovery and quantitation of proteins
    • Carraro, U., Rizzi, C., Sandri, M. and Doria, D., A new two-step precipitation method removes free-SDS and thiol reagents from diluted solutions, and then allows recovery and quantitation of proteins. Biochem. Biophys. Res. Commun., 1994, 200, 916-924.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 916-924
    • Carraro, U.1    Rizzi, C.2    Sandri, M.3    Doria, D.4
  • 4
    • 0001547429 scopus 로고
    • Major proteins of beer and their precursor in barley: Electrophoretic and immunological studies
    • Curioni, A., Pressi, G., Furegon, L. and Peruffo, A., Major proteins of beer and their precursor in barley: electrophoretic and immunological studies. J. Agric. Food. Chem., 1995, 43, 2620-2626.
    • (1995) J. Agric. Food. Chem. , vol.43 , pp. 2620-2626
    • Curioni, A.1    Pressi, G.2    Furegon, L.3    Peruffo, A.4
  • 7
    • 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
  • 8
    • 84979404818 scopus 로고
    • Purification and properties of major antigenic beer protein of barley origin
    • Hejgaard, J. and Kaersgaard, P., Purification and properties of major antigenic beer protein of barley origin. J. Inst. Brew., 1983, 89(6), 402-410.
    • (1983) J. Inst. Brew. , vol.89 , Issue.6 , pp. 402-410
    • Hejgaard, J.1    Kaersgaard, P.2
  • 9
    • 84979400255 scopus 로고
    • Antigenic beer macromolecules - An experimental survey of purification methods
    • Kaersgaard, P. and Hejgaard, J., Antigenic beer macromolecules - an experimental survey of purification methods. J. Inst. Brew., 1979, 85, 103-111.
    • (1979) J. Inst. Brew. , vol.85 , pp. 103-111
    • Kaersgaard, P.1    Hejgaard, J.2
  • 10
    • 84988159811 scopus 로고
    • Isolation of beer foam polypeptides by Hydrophobic interaction chromatography and their partial characterization
    • Onishi, A. and Proudlove, M.O., Isolation of beer foam polypeptides by Hydrophobic interaction chromatography and their partial characterization. J. Sci. Food Agric., 1994, 65, 233-240.
    • (1994) J. Sci. Food Agric. , vol.65 , pp. 233-240
    • Onishi, A.1    Proudlove, M.O.2
  • 11
    • 0038322685 scopus 로고    scopus 로고
    • The gel filtration chromatographic-profiles of proteins and peptides of wort and beer: Effect of processing - Malting, mashing, kettle boiling, fermentation and filtering
    • Osman, A.M., Coverdale, S.M., Onley-Watson, K., Bell, B. and Healy, P., The gel filtration chromatographic-profiles of proteins and peptides of wort and beer: effect of processing - malting, mashing, kettle boiling, fermentation and filtering. J. Inst. Brew., 2003, 109, 41-50.
    • (2003) J. Inst. Brew. , vol.109 , pp. 41-50
    • Osman, A.M.1    Coverdale, S.M.2    Onley-Watson, K.3    Bell, B.4    Healy, P.5
  • 12
    • 0036709123 scopus 로고    scopus 로고
    • Fully reversible procedure for silver staining improves densitometry of complex mixtures of biopolymers resolved by sodium dodecyl sulfate- polyacrylamide gel electrophoesis
    • Rizzi, C., Rossini, K., Bruson, A., Sandri, M., Dal Belin Peruffo, A. and Carraro, U., Fully reversible procedure for silver staining improves densitometry of complex mixtures of biopolymers resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoesis. Electrophoresis, 2002, 23, 3266-3269.
    • (2002) Electrophoresis , vol.23 , pp. 3266-3269
    • Rizzi, C.1    Rossini, K.2    Bruson, A.3    Sandri, M.4    Dal Belin Peruffo, A.5    Carraro, U.6
  • 13
    • 0038120676 scopus 로고    scopus 로고
    • Electrophoretic methods in the analysis of beverage
    • Sàdeckà, J. and Polonsky, J., Electrophoretic methods in the analysis of beverage. J. Chromatogr. A, 2000, 880, 243-279.
    • (2000) J. Chromatogr. A , vol.880 , pp. 243-279
    • Sàdeckà, J.1    Polonsky, J.2
  • 14
    • 0001557431 scopus 로고
    • Small and large scale preparative purification of myosin light and heavy chains by selective KDS precipitation of myosin subunits: Yield by SDS PAGE and quantitative orthogonal densitometry
    • Sandri, M., Rizzi, C., Catani, C. and Carraro, U., Small and large scale preparative purification of myosin light and heavy chains by selective KDS precipitation of myosin subunits: Yield by SDS PAGE and quantitative orthogonal densitometry. Basic Appl. Myol., 1992, 2, 107-114.
    • (1992) Basic Appl. Myol. , vol.2 , pp. 107-114
    • Sandri, M.1    Rizzi, C.2    Catani, C.3    Carraro, U.4
  • 15
    • 84979424803 scopus 로고
    • The fractionation of polypeptides from barley and beer by hydrophobic interaction chromatography: The influence of their hydrophobicity on foam stability
    • Slack, P.T. and Bamforth, C.W., The fractionation of polypeptides from barley and beer by hydrophobic interaction chromatography: the influence of their hydrophobicity on foam stability. J. Inst. Brew., 1983, 89, 397-401.
    • (1983) J. Inst. Brew. , vol.89 , pp. 397-401
    • Slack, P.T.1    Bamforth, C.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.