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Volumn 60, Issue 17, 2012, Pages 4320-4326

Proteome profiling of seed storage proteins reveals the nutritional potential of Salicornia brachiata Roxb., an extreme halophyte

Author keywords

2D gel; globulins; MALDI TOF; peptide fingerprinting; Salicornia; seed protein

Indexed keywords

DIETARY SUPPLEMENTATION; DIFFERENT SOLVENTS; DISTILLED WATER; DISULFIDE LINKAGES; GLOBULINS; ISO-ELECTRIC POINTS; MALDI TOF MS; MALDI-TOF; MATRIX ASSISTED LASER DESORPTION; NUTRITIONAL VALUE; PEPTIDE MASS FINGERPRINT; POTENTIAL SOURCES; PROTEIN SPOTS; PROTEOME PROFILING; REGULATORY PROTEIN; SALICORNIA; SDS-PAGE; SEED PROTEIN; SEED STORAGE PROTEINS; SEQUENTIAL EXTRACTION; TWO-DIMENSIONAL GELS;

EID: 84860490791     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf203632v     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 11244271039 scopus 로고    scopus 로고
    • Food and Agriculture Organization of the United Nations (FAO): Rome, Italy, (accessed June 22, 2011).
    • The State of Food and Agriculture 2003-2004; Food and Agriculture Organization of the United Nations (FAO): Rome, Italy, 2004; http://www.fao.org/docrep/006/Y5160E/Y5160E00.htm (accessed June 22, 2011).
    • (2004) The State of Food and Agriculture 2003-2004
  • 2
    • 1142281833 scopus 로고    scopus 로고
    • Improving crop salt tolerance
    • DOI 10.1093/jxb/erh003
    • Flowers, T. J. Improving crop salt tolerance J. Exp. Bot. 2004, 55, 307-319 (Pubitemid 38204113)
    • (2004) Journal of Experimental Botany , vol.55 , Issue.396 , pp. 307-319
    • Flowers, T.J.1
  • 3
    • 0032943919 scopus 로고    scopus 로고
    • Salt tolerance and crop potential of halophytes
    • DOI 10.1016/S0735-2689(99)00388-3
    • Glenn, E.; Brown, J.; Blumwald, E. Salt tolerance and crop potential of halophytes Crit. Rev. Plant Sci. 1999, 18, 227-255 (Pubitemid 29178178)
    • (1999) Critical Reviews in Plant Sciences , vol.18 , Issue.2 , pp. 227-255
    • Glenn, E.P.1    Brown, J.J.2    Blumwald, E.3
  • 4
    • 67650079928 scopus 로고    scopus 로고
    • Identification of salt-induced genes from Salicornia brachiata, an extreme halophyte through expressed sequence tags analysis
    • Jha, B.; Agarwal, P. K.; Reddy, P. S.; Lal, S.; Sopory, S. K.; Reddy, M. K. Identification of salt-induced genes from Salicornia brachiata, an extreme halophyte through expressed sequence tags analysis Genes Genet. Sys. 2009, 84, 111-120
    • (2009) Genes Genet. Sys. , vol.84 , pp. 111-120
    • Jha, B.1    Agarwal, P.K.2    Reddy, P.S.3    Lal, S.4    Sopory, S.K.5    Reddy, M.K.6
  • 5
    • 49649129752 scopus 로고    scopus 로고
    • A study on salicornia (S. brachiata Roxb.) in salinity ingressed soils of India
    • Pandya, J. B.; Gohil, R. H.; Patolia, J. S.; Shah, M. T.; Parmar, D. R. A study on salicornia (S. brachiata Roxb.) in salinity ingressed soils of India Int. J. Agric. Res. 2006, 1, 91-99
    • (2006) Int. J. Agric. Res. , vol.1 , pp. 91-99
    • Pandya, J.B.1    Gohil, R.H.2    Patolia, J.S.3    Shah, M.T.4    Parmar, D.R.5
  • 6
    • 25144502782 scopus 로고    scopus 로고
    • Alcoholysis of salicornia oil using free and covalently bound lipase onto chitosan beads
    • DOI 10.1016/j.foodchem.2004.12.030, PII S0308814605000440
    • Desai, P. D.; Dave, A. M.; Devi, S. Alcoholysis of salicornia oil using free and covalently bound lipase onto chitosan beads Food Chem. 2006, 95, 193-199 (Pubitemid 41338155)
    • (2006) Food Chemistry , vol.95 , Issue.2 , pp. 193-199
    • Desai, P.D.1    Dave, A.M.2    Devi, S.3
  • 7
    • 80051918796 scopus 로고    scopus 로고
    • Bioprospecting marine halophyte Salicornia brachiata for medical importance and salt encrusted land development
    • Stanley, O. D. Bioprospecting marine halophyte Salicornia brachiata for medical importance and salt encrusted land development J. Coastal Dev. 2008, 11, 62-69
    • (2008) J. Coastal Dev. , vol.11 , pp. 62-69
    • Stanley, O.D.1
  • 9
    • 0001862611 scopus 로고    scopus 로고
    • Irrigating crops with seawater
    • Glenn, E. P.; Brown, J.; O'Leary, J. Irrigating crops with seawater Sci. Am. 1998, 279, 76-81
    • (1998) Sci. Am. , vol.279 , pp. 76-81
    • Glenn, E.P.1    Brown, J.2    O'Leary, J.3
  • 10
    • 0034071916 scopus 로고    scopus 로고
    • Critical phosphorus levels for Salicornia growth
    • Alsaeedi, A. H.; Elprince, A. M. Critical phosphorus levels for Salicornia growth Agron. J. 2000, 92, 336-345 (Pubitemid 30308636)
    • (2000) Agronomy Journal , vol.92 , Issue.2 , pp. 336-345
    • Alsaeedi, A.H.1    Elprince, A.M.2
  • 12
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire, E.; Wright, D. J.; Boulter, D. Legumin and vicilin, storage proteins of legume seeds Phytochemistry 1976, 15, 3-24
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 15
    • 0041377474 scopus 로고
    • Pumpkin (Cucurbita sp) seed globulins III: Comparison of subunit structures among seed globulins of various Cucurbita species and characterization of peptide components
    • Hara, I.; Ohmiya, M.; Matsubara, H. Pumpkin (Cucurbita sp) seed globulins III: comparison of subunit structures among seed globulins of various Cucurbita species and characterization of peptide components Plant Cell Physiol. 1978, 19, 237-243
    • (1978) Plant Cell Physiol. , vol.19 , pp. 237-243
    • Hara, I.1    Ohmiya, M.2    Matsubara, H.3
  • 16
    • 0025100581 scopus 로고
    • Characterization of matteuccin, the 2.2S storage protein of the ostrich fern. Evolutionary relationship to angiosperm seed storage proteins
    • DOI 10.1111/j.1432-1033.1990.tb19201.x
    • Rodin, J.; Rask, L. Characterization of matteuccin, the 2.2s storage protein of the ostrich fern: evolutionary relationship to angiosperm seed storage proteins Eur. J. Biochem. 1990, 192, 101-107 (Pubitemid 20277512)
    • (1990) European Journal of Biochemistry , vol.192 , Issue.1 , pp. 101-107
    • Rodin, J.1    Rask, L.2
  • 17
    • 0001424466 scopus 로고
    • Oat seed globulin: Subunit characterization and demonstration of its synthesis as a precursor
    • Walburg, G.; Larkins, B. A. Oat seed globulin: subunit characterization and demonstration of its synthesis as a precursor Plant Physiol. 1983, 72, 161-165
    • (1983) Plant Physiol. , vol.72 , pp. 161-165
    • Walburg, G.1    Larkins, B.A.2
  • 18
    • 0022826151 scopus 로고
    • Structure of the rapeseed 1.7 S storage protein, napin, and its precursor
    • Ericson, M.; Rödin, J.; Lenman, M.; Glimelius, K.; Josefsson, L. G.; Rask, L. Structure of the rapeseed 1.7S storage protein, napin, and its precursor J. Biol. Chem. 1986, 261, 14576-14581 (Pubitemid 17220246)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.31 , pp. 14576-14581
    • Ericson, M.L.1    Rodin, J.2    Lenman, M.3
  • 19
    • 0000932242 scopus 로고
    • Seed storage proteins
    • Stumpf, P. K. Conn, E. E. Academic Press: New York
    • Larkins, B. A. Seed storage proteins. In Biochemistry of Plants: A Comprehensive Treatse; Stumpf, P. K.; Conn, E. E., Eds.; Academic Press: New York, 1981; pp 449-489.
    • (1981) Biochemistry of Plants: A Comprehensive Treatse , pp. 449-489
    • Larkins, B.A.1
  • 20
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants
    • Hoffman, L. M.; Donaldson, D. D.; Herman, E. M. A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants Plant Mol. Biol. 1988, 11, 717-729
    • (1988) Plant Mol. Biol. , vol.11 , pp. 717-729
    • Hoffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 21
    • 0027087211 scopus 로고
    • Molecular cloning of a gene encoding a seed-specific protein with nutritionally balanced amino acid composition from Amaranthus
    • DOI 10.1073/pnas.89.24.11774
    • Raina, A.; Datta, A. Molecular cloning of a gene encoding a seed specific protein with nutritionally balanced amino acid composition from Amaranthus Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 11774-11778 (Pubitemid 23004726)
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , Issue.24 , pp. 11774-11778
    • Raina, A.1    Datta, A.2
  • 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. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0003069796 scopus 로고
    • The general properties, classification and distribution of plant proteins
    • Norton, G. Butterworth: London. U.K.
    • Boulter, D.; Derbyshire, E. The general properties, classification and distribution of plant proteins. In Plant Proteins; Norton, G., Ed.; Butterworth: London. U.K., 1978; pp 3-24.
    • (1978) Plant Proteins , pp. 3-24
    • Boulter, D.1    Derbyshire, E.2
  • 24
    • 33746577494 scopus 로고    scopus 로고
    • Concepts and approaches towards understanding the cellular redox proteome
    • DOI 10.1055/s-2006-923961
    • Stroher, E.; Dietz, K. J. Concepts and approaches towards understanding the cellular redox proteome Plant Biol. 2006, 8, 407-418 (Pubitemid 44140734)
    • (2006) Plant Biology , vol.8 , Issue.4 , pp. 407-418
    • Stroher, E.1    Dietz, K.-J.2
  • 25
    • 0016187789 scopus 로고
    • Purification and subunit structure of legumin of Vicia faba L. (broad bean)
    • Wright, D. J.; Boulter, D. Purification and subunit structure of legumin of Vicia faba L. (broad bean) Biochem. J. 1974, 141, 413-418
    • (1974) Biochem. J. , vol.141 , pp. 413-418
    • Wright, D.J.1    Boulter, D.2
  • 26
    • 77956981115 scopus 로고
    • The structure of legumin of Vicia faba - A reappraisal
    • Matta, N. K.; Gatehouse, J. A.; Boulter, D. The structure of legumin of Vicia faba - a reappraisal J. Exp. Bot. 1981, 32, 83-197
    • (1981) J. Exp. Bot. , vol.32 , pp. 83-197
    • Matta, N.K.1    Gatehouse, J.A.2    Boulter, D.3
  • 27
    • 0041943155 scopus 로고    scopus 로고
    • Purification and characterization of legumin and vicilin of Lathyrus sativus L
    • Chandna, M.; Matta, N. K. Purification and characterization of legumin and vicilin of Lathyrus sativus L Physiol. Mol. Biol. Plants 1999, 5, 139-144
    • (1999) Physiol. Mol. Biol. Plants , vol.5 , pp. 139-144
    • Chandna, M.1    Matta, N.K.2
  • 28
    • 54349097685 scopus 로고    scopus 로고
    • Variation studies on seed storage proteins and phylogenetics of the genus Cucumis
    • Singh, N. P.; Matta, N. K. Variation studies on seed storage proteins and phylogenetics of the genus Cucumis Plant Sys. Evol. 2008, 275, 209-218
    • (2008) Plant Sys. Evol. , vol.275 , pp. 209-218
    • Singh, N.P.1    Matta, N.K.2
  • 29
    • 0032033440 scopus 로고    scopus 로고
    • +-atpase to generate a fusicoccin binding complex and a fusicoccin responsive system
    • DOI 10.1046/j.1365-313X.1998.00083.x
    • Baunsgaard, L.; Fuglsang, A. T.; Jahn, T.; Korthout, H. A. A. J.; deBoer, A. H.; Palmgren, M. G. The 14-3-3 proteins associate with the plant plasma membrane H1-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system Plant J. 1998, 13, 661-671 (Pubitemid 28178492)
    • (1998) Plant Journal , vol.13 , Issue.5 , pp. 661-671
    • Baunsgaard, L.1    Fuglsang, A.T.2    Jahn, T.3    Korthout, H.A.A.J.4    De Boer, A.H.5    Palmgren, M.G.6
  • 30
    • 0030920840 scopus 로고    scopus 로고
    • Multiple signals and mechanisms that regulate leaf growth and stomatal behaviour during water deficit
    • DOI 10.1034/j.1399-3054.1997.1000212.x
    • Thompson, D. S.; Wilkinson, S.; Bacon, M. A.; Davies, W. J. Multiple signals and mechanisms that regulate leaf growth and stomatal behaviour during water deficit Physiol. Plant. 1997, 100, 303-313 (Pubitemid 27274907)
    • (1997) Physiologia Plantarum , vol.100 , Issue.2 , pp. 303-313
    • Thompson, D.S.1    Wilkinson, S.2    Bacon, M.A.3    Davies, W.J.4
  • 31
    • 0026504452 scopus 로고
    • Xyloglucan endotransglycosylase, a new wall-loosening enzyme activity from plants
    • Fry, S. C.; Smith, R. C.; Renwick, K. F.; Martin, D. J.; Hodge, S. K.; Matthews, K. J. Xyloglucan endotransglycosylase, a new wall-loosening enzyme activity from plants Biochem. J. 1992, 282, 821-828
    • (1992) Biochem. J. , vol.282 , pp. 821-828
    • Fry, S.C.1    Smith, R.C.2    Renwick, K.F.3    Martin, D.J.4    Hodge, S.K.5    Matthews, K.J.6
  • 32
    • 0026640666 scopus 로고
    • Endoxyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule
    • Nishitani, K.; Tominaga, R. Endoxyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule J. Biol. Chem. 1992, 267, 21058-21064
    • (1992) J. Biol. Chem. , vol.267 , pp. 21058-21064
    • Nishitani, K.1    Tominaga, R.2
  • 33
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse ceil functions
    • Bourne, H. R.; Sander, D. A.; McCormick, F. The GTPase superfamily: a conserved switch for diverse ceil functions Nature (London) 1990, 348, 125-132
    • (1990) Nature (London) , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sander, D.A.2    McCormick, F.3
  • 34
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R.; Sanders, D. A.; Mcrmick, F. The GTPase superfamily: conserved structure and molecular mechanism Nature 1991, 349, 117-127 (Pubitemid 21912023)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 35
    • 0028702491 scopus 로고
    • GTP-binding proteins in plants: New members of an old family
    • Ma, H. GTP-binding proteins in plants: new members of an old family Plant Mol. Biol. 1994, 26, 1611-1636
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1611-1636
    • Ma, H.1
  • 36
    • 0029974453 scopus 로고    scopus 로고
    • Extra ribosomal functions of ribosomal proteins
    • Wool, I. G. Extra ribosomal functions of ribosomal proteins Trends Biochem. Sci. 1996, 21, 164-165
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 164-165
    • Wool, I.G.1
  • 39
    • 0029303181 scopus 로고
    • A cDNA encoding ribosomal protein S4e from cotton (Gossypium hirsutum L)
    • Turley, R. B.; Ferguson, D. L.; Meredith, W. R., Jr. A cDNA encoding ribosomal protein S4e from cotton (Gossypium hirsutum L) Plant Physiol. 1995, 108, 431-432
    • (1995) Plant Physiol. , vol.108 , pp. 431-432
    • Turley, R.B.1    Ferguson, D.L.2    Meredith Jr., W.R.3
  • 40
    • 0000908641 scopus 로고
    • A new member of the CAB gene family: Structure, expression and chromosomal location of Cab-8, the tomato gene encoding the type III chlorophyll a/b-binding polypeptide of photosystem i
    • Pichersky, E.; Brock, T. G.; Nguyen, D.; Hoffman, N. E.; Piechulla, B.; Tanksley, S. D.; Green, B. R. A new member of the CAB gene family: structure, expression and chromosomal location of Cab-8, the tomato gene encoding the type III chlorophyll a/b-binding polypeptide of photosystem I Plant Mol. Biol. 1989, 12, 257-270
    • (1989) Plant Mol. Biol. , vol.12 , pp. 257-270
    • Pichersky, E.1    Brock, T.G.2    Nguyen, D.3    Hoffman, N.E.4    Piechulla, B.5    Tanksley, S.D.6    Green, B.R.7
  • 41
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • DOI 10.1016/j.bbabio.2004.09.009, PII S0005272804002749
    • Dekker, J. P.; Boekema, E. J. Supramolecular organization of thylakoid membrane proteins in green plants Biochim. Biophys. Acta 2005, 1706, 12-39 (Pubitemid 40044704)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 42
    • 0000541912 scopus 로고
    • The detection, isolation and characterization of a light-harvesting complex which is specifically associated with photosystem i
    • Haworth, P.; Watson, J. L.; Arntzen, C. J. The detection, isolation and characterization of a light-harvesting complex which is specifically associated with photosystem I Biochim. Biophys. Acta 1983, 724, 151-158
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 151-158
    • Haworth, P.1    Watson, J.L.2    Arntzen, C.J.3


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