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Volumn 91, Issue 4, 2005, Pages 447-459

Industrial process proteomics: Alfalfa protein patterns during wet fractionation processing

Author keywords

2 D electrophoresis, mass spectrometry; Homology based proteomic analysis; Medicago sativa; Wet fractionation process

Indexed keywords

BIOMASS; MASS SPECTROMETRY; PLANTS (BOTANY);

EID: 23244454136     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20520     Document Type: Article
Times cited : (11)

References (50)
  • 1
    • 0036668514 scopus 로고    scopus 로고
    • Analytical and biological variances associated with proteomic studies of Medicago truncatula by two-dimensional polyacrylamide gel electrophoresis
    • Asirvatham VS, Watson BS, Sumner LW. 2002. Analytical and biological variances associated with proteomic studies of Medicago truncatula by two-dimensional polyacrylamide gel electrophoresis. Proteomics 2(8): 960-968.
    • (2002) Proteomics , vol.2 , Issue.8 , pp. 960-968
    • Asirvatham, V.S.1    Watson, B.S.2    Sumner, L.W.3
  • 5
    • 33947293254 scopus 로고
    • PRO-XAN process: Design and evaluation of a pilot plant system for the coagulation and separation of the leaf protein from alfalfa juice
    • Bickoff EM, Spencer RR, Mottola AC, Clark JP, O KG. 1971. PRO-XAN process: Design and evaluation of a pilot plant system for the coagulation and separation of the leaf protein from alfalfa juice. J Agr Food Chem 19(3):504-507.
    • (1971) J Agr Food Chem , vol.19 , Issue.3 , pp. 504-507
    • Bickoff, E.M.1    Spencer, R.R.2    Mottola, A.C.3    Clark, J.P.4
  • 6
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston RS, Viitanen PV, Vierling E. 1996. Molecular chaperones and protein folding in plants. Plant Mol Biol 32:191-222.
    • (1996) Plant Mol Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 7
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(7):248-254.
    • (1976) Anal Biochem , vol.72 , Issue.7 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0034144393 scopus 로고    scopus 로고
    • Patterns of protein synthesis and tolerance of anoxia in root tips of maize seedlings acclimated to a low-oxygen environment, and identification of proteins by mass spectrometry
    • Chang WW, Huang L, Shen M, Webster C, Burlingame AL, Roberts JK. 2000. Patterns of protein synthesis and tolerance of anoxia in root tips of maize seedlings acclimated to a low-oxygen environment, and identification of proteins by mass spectrometry. Plant Physiol 122(2):295-318.
    • (2000) Plant Physiol , vol.122 , Issue.2 , pp. 295-318
    • Chang, W.W.1    Huang, L.2    Shen, M.3    Webster, C.4    Burlingame, A.L.5    Roberts, J.K.6
  • 9
    • 0031400786 scopus 로고    scopus 로고
    • The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature
    • Crafts-Brandner SJ, Van De Loo FJ, Salvucci ME. 1997. The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature. Plant Physiol 114(2):439-444.
    • (1997) Plant Physiol , vol.114 , Issue.2 , pp. 439-444
    • Crafts-Brandner, S.J.1    Van De Loo, F.J.2    Salvucci, M.E.3
  • 10
    • 6344231099 scopus 로고
    • True metabolizable energy and true amino acid availability of an alfalfa protein concentrate (Pro-Xan)
    • Dale NM, Fuller HL, Halloran HR. 1984. True metabolizable energy and true amino acid availability of an alfalfa protein concentrate (Pro-Xan). Poultry Sci 63(2):388-390.
    • (1984) Poultry Sci , vol.63 , Issue.2 , pp. 388-390
    • Dale, N.M.1    Fuller, H.L.2    Halloran, H.R.3
  • 11
    • 0034281801 scopus 로고    scopus 로고
    • Effect of PDI overexpression on recombinant protein secretion in CHO cells
    • Davis R, Schooley K, Rasmussen B, Thomas J, Reddy P. 2000. Effect of PDI overexpression on recombinant protein secretion in CHO cells. Biotechnol Prog 16(5):736-743.
    • (2000) Biotechnol Prog , vol.16 , Issue.5 , pp. 736-743
    • Davis, R.1    Schooley, K.2    Rasmussen, B.3    Thomas, J.4    Reddy, P.5
  • 13
    • 0031040836 scopus 로고    scopus 로고
    • Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) and rubisco activase and the inability of rubisco activase to restore activity of heat-denatured rubisco
    • Eckardt NA, Portis AR, Jr. 1997. Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) and rubisco activase and the inability of rubisco activase to restore activity of heat-denatured rubisco. Plant Physiol 113(1):243-248.
    • (1997) Plant Physiol , vol.113 , Issue.1 , pp. 243-248
    • Eckardt, N.A.1    Portis Jr., A.R.2
  • 15
    • 4644232679 scopus 로고    scopus 로고
    • Folding-promoting agents in recombinant protein production
    • Fahnert B. 2004. Folding-promoting agents in recombinant protein production. Methods Mol Biol 267:53-74.
    • (2004) Methods Mol Biol , vol.267 , pp. 53-74
    • Fahnert, B.1
  • 16
    • 0035059453 scopus 로고    scopus 로고
    • Medicago truncatula on the move!
    • Frugoli J, Harris J. 2001. Medicago truncatula on the move! Plant Cell 13(3):458-463.
    • (2001) Plant Cell , vol.13 , Issue.3 , pp. 458-463
    • Frugoli, J.1    Harris, J.2
  • 17
    • 0345873538 scopus 로고    scopus 로고
    • Assessing matrix assisted laser desorption/ionization-time of flight-mass spectrometry as a means of rapid embryo protein identification in rice
    • Fukuda M, Islam N, Woo SH, Yamagishi A, Takaoka M, Hirano H. 2003. Assessing matrix assisted laser desorption/ionization-time of flight-mass spectrometry as a means of rapid embryo protein identification in rice. Electrophoresis 24(7-8):1319-1329.
    • (2003) Electrophoresis , vol.24 , Issue.7-8 , pp. 1319-1329
    • Fukuda, M.1    Islam, N.2    Woo, S.H.3    Yamagishi, A.4    Takaoka, M.5    Hirano, H.6
  • 18
    • 0034696469 scopus 로고    scopus 로고
    • Expression of a Solanum tuberosum cyclophilin gene is regulated by fungal infection and abiotic stress conditions
    • Godoy AV, Lazzaro AS, Casalongué CA, San Segundo B. 2000. Expression of a Solanum tuberosum cyclophilin gene is regulated by fungal infection and abiotic stress conditions. Plant Sci 152(2):123-134.
    • (2000) Plant Sci , vol.152 , Issue.2 , pp. 123-134
    • Godoy, A.V.1    Lazzaro, A.S.2    Casalongué, C.A.3    San Segundo, B.4
  • 19
  • 20
    • 16344375379 scopus 로고    scopus 로고
    • Characterisation of rice anther proteins expressed at the young microspore stage
    • Imin N, Kerim T, Weinman JJ, Rolfe BG. 2001. Characterisation of rice anther proteins expressed at the young microspore stage. Proteomics 1(9):1149-1161.
    • (2001) Proteomics , vol.1 , Issue.9 , pp. 1149-1161
    • Imin, N.1    Kerim, T.2    Weinman, J.J.3    Rolfe, B.G.4
  • 23
    • 33644488250 scopus 로고
    • PRO-XAN[protein-xanthophyll] process. Pilot plant for separation of heat-precipitated leaf protein from residual alfalfa juice
    • Lazar ME, Spencer RR, Knuckles BE, Bickoff EM. 1971. PRO-XAN[protein- xanthophyll] process. Pilot plant for separation of heat-precipitated leaf protein from residual alfalfa juice. J Agr Food Chem 19(5):944-946.
    • (1971) J Agr Food Chem , vol.19 , Issue.5 , pp. 944-946
    • Lazar, M.E.1    Spencer, R.R.2    Knuckles, B.E.3    Bickoff, E.M.4
  • 24
    • 0036807946 scopus 로고    scopus 로고
    • Comparative bioinformatic analysis of complete proteomes and protein parameters for cross-species identification in proteomics
    • Lester PJ, Hubbard SJ. 2002. Comparative bioinformatic analysis of complete proteomes and protein parameters for cross-species identification in proteomics. Proteomics 2(10):1392-1405.
    • (2002) Proteomics , vol.2 , Issue.10 , pp. 1392-1405
    • Lester, P.J.1    Hubbard, S.J.2
  • 25
    • 0041663955 scopus 로고    scopus 로고
    • Study of human laryngeal muscle protein using two-dimensional electrophoresis and mass spectrometry
    • Li ZB, Lehar M, Braga N, Westra W, Liu LH, Flint PW. 2003. Study of human laryngeal muscle protein using two-dimensional electrophoresis and mass spectrometry. Proteomics 3(7):1325-1334.
    • (2003) Proteomics , vol.3 , Issue.7 , pp. 1325-1334
    • Li, Z.B.1    Lehar, M.2    Braga, N.3    Westra, W.4    Liu, L.H.5    Flint, P.W.6
  • 26
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: Cross-species protein identification by mass spectrometry and its implications
    • Liska AJ, Shevchenko A. 2003. Expanding the organismal scope of proteomics: Cross-species protein identification by mass spectrometry and its implications. Proteomics 3(1):19-28.
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 28
    • 0035525061 scopus 로고    scopus 로고
    • Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting
    • Mathesius U, Keijzers G, Natera SH, Weinman JJ, Djordjevic MA, Rolfe BG. 2001. Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics 1(11):1424-1440.
    • (2001) Proteomics , vol.1 , Issue.11 , pp. 1424-1440
    • Mathesius, U.1    Keijzers, G.2    Natera, S.H.3    Weinman, J.J.4    Djordjevic, M.A.5    Rolfe, B.G.6
  • 29
    • 0033230242 scopus 로고    scopus 로고
    • Protein folding in the plant cell
    • Miernyk JA. 1999. Protein folding in the plant cell. Plant Physiol 121(3): 695-703.
    • (1999) Plant Physiol , vol.121 , Issue.3 , pp. 695-703
    • Miernyk, J.A.1
  • 30
    • 0027460652 scopus 로고
    • Removal of N-terminal formyl groups and deblocking of pyrrolidone carboxylic acid of proteins with anhydrous hydrazine vapor
    • Miyatake N, Kamo M, Satake K, Uchiyama Y, Tsugita A. 1993. Removal of N-terminal formyl groups and deblocking of pyrrolidone carboxylic acid of proteins with anhydrous hydrazine vapor. Eur J Biochem 212(3):785-789.
    • (1993) Eur J Biochem , vol.212 , Issue.3 , pp. 785-789
    • Miyatake, N.1    Kamo, M.2    Satake, K.3    Uchiyama, Y.4    Tsugita, A.5
  • 31
    • 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. 1988. 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 9(6):255-262.
    • (1988) Electrophoresis , vol.9 , Issue.6 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 32
    • 0032189170 scopus 로고    scopus 로고
    • Purification and characterization of an endoprotease from alfalfa senescent leaves
    • Nieri B, Canino S, Versace R, Alpi A. 1998. Purification and characterization of an endoprotease from alfalfa senescent leaves. Phytochem 49(3): 643-649.
    • (1998) Phytochem , vol.49 , Issue.3 , pp. 643-649
    • Nieri, B.1    Canino, S.2    Versace, R.3    Alpi, A.4
  • 33
    • 0035987498 scopus 로고    scopus 로고
    • Initial proteome analysis of mature barley seeds and malt
    • Ostergaard O, Melchior S, Roepstorff P, Svensson B. 2002. Initial proteome analysis of mature barley seeds and malt. Proteomics 2(6):733-739.
    • (2002) Proteomics , vol.2 , Issue.6 , pp. 733-739
    • Ostergaard, O.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 34
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier JB, Friso G, Kalume DE, Roepstorff P, Nilsson F, Adamska I, van Wijk KJ. 2000. Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12(3):319-341.
    • (2000) Plant Cell , vol.12 , Issue.3 , pp. 319-341
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5    Adamska, I.6    Van Wijk, K.J.7
  • 36
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase-Rubisco's catalytic chaperone
    • Portis ARJ. 2003. Rubisco activase-Rubisco's catalytic chaperone. Photosynth Res75(1):11-27.
    • (2003) Photosynth Res , vol.75 , Issue.1 , pp. 11-27
    • Portis, A.R.J.1
  • 37
    • 63249119658 scopus 로고    scopus 로고
    • The proteome of maize leaves: Use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints
    • Porubleva L, Vander Velden K, Kothari S, Oliver DJ, Chitnis PR. 2001. The proteome of maize leaves: Use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints. Electrophoresis 22(9):1724-1738.
    • (2001) Electrophoresis , vol.22 , Issue.9 , pp. 1724-1738
    • Porubleva, L.1    Vander Velden, K.2    Kothari, S.3    Oliver, D.J.4    Chitnis, P.R.5
  • 40
    • 0021989672 scopus 로고
    • Complete amino acid sequence of human hemopexin, the heme-binding protein of serum
    • Takahashi N, Takahashi Y, Putnam FW. 1985. Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. Proc Natl Acad Sci USA 82(1):73-77.
    • (1985) Proc Natl Acad Sci USA , vol.82 , Issue.1 , pp. 73-77
    • Takahashi, N.1    Takahashi, Y.2    Putnam, F.W.3
  • 41
    • 0034987772 scopus 로고    scopus 로고
    • Challenges and prospects of plant proteomics
    • Van Wijk KJ. 2001. Challenges and prospects of plant proteomics. Plant Physiol 126:501-508.
    • (2001) Plant Physiol , vol.126 , pp. 501-508
    • Van Wijk, K.J.1
  • 44
    • 0042367748 scopus 로고    scopus 로고
    • Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae
    • Wang W, Sun J, Hartlep M, Deckwer WD, Zeng AP. 2003. Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae. Biotechnol Bioeng 83(5):525-536.
    • (2003) Biotechnol Bioeng , vol.83 , Issue.5 , pp. 525-536
    • Wang, W.1    Sun, J.2    Hartlep, M.3    Deckwer, W.D.4    Zeng, A.P.5
  • 45
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters ER, Lee GJ, Vierling E. 1996. Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 47(296):325-338.
    • (1996) J Exp Bot , vol.47 , Issue.296 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 46
    • 0037353383 scopus 로고    scopus 로고
    • Mapping the proteome of barrel medic (Medicago truncatula)
    • Watson BS, Asirvatham VS, Wang L, Sumner LW. 2003. Mapping the proteome of barrel medic (Medicago truncatula). Plant Physiol 131(3): 1104-1123.
    • (2003) Plant Physiol , vol.131 , Issue.3 , pp. 1104-1123
    • Watson, B.S.1    Asirvatham, V.S.2    Wang, L.3    Sumner, L.W.4
  • 48
    • 0025250323 scopus 로고
    • Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine
    • Wellner D, Panneerselvam C, Horecker BL. 1990. Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine. Proc Natl Acad Sci USA 87(5):1947-1949.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.5 , pp. 1947-1949
    • Wellner, D.1    Panneerselvam, C.2    Horecker, B.L.3
  • 50
    • 0037879092 scopus 로고    scopus 로고
    • A reference map of a human pituitary adenoma proteome
    • Zhan X, Desiderio DM. 2003. A reference map of a human pituitary adenoma proteome. Proteomics 3(5):699-713.
    • (2003) Proteomics , vol.3 , Issue.5 , pp. 699-713
    • Zhan, X.1    Desiderio, D.M.2


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