메뉴 건너뛰기




Volumn 18, Issue 3, 2004, Pages 327-341

Hull-less barley varieties: Storage proteins and amino acid distribution in relation to nutritional quality

Author keywords

Lysine; Prolamins; Storage proteins; Threonine

Indexed keywords

AMINO ACIDS; GENETIC ENGINEERING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NUTRITION; PROTEINS;

EID: 9944265796     PISSN: 08905436     EISSN: None     Source Type: Journal    
DOI: 10.1081/FBT-200040531     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 0003905660 scopus 로고
    • St. Paul, Minnesota
    • AACC - American Association of Cereal Chemists. (1995). Approved Methods. 9th ed. St. Paul, Minnesota.
    • (1995) Approved Methods. 9th Ed.
  • 2
    • 0035989811 scopus 로고    scopus 로고
    • Analysis of the aspartic acid metabolic pathway using mutant Genes
    • Azevedo, R. A. (2002). Analysis of the aspartic acid metabolic pathway using mutant Genes. Amino Acids 22:217-230.
    • (2002) Amino Acids , vol.22 , pp. 217-230
    • Azevedo, R.A.1
  • 3
    • 0035094676 scopus 로고    scopus 로고
    • Lysine metabolism in higher plants
    • Azevedo, R. A., Lea, P. J. (2001). Lysine metabolism in higher plants. Amino Acids 20:261-279.
    • (2001) Amino Acids , vol.20 , pp. 261-279
    • Azevedo, R.A.1    Lea, P.J.2
  • 4
    • 0002599959 scopus 로고
    • Biochemical genetics of the interaction of the lysine plus threonine resistant mutant Ltr*19 with opaque-2 maize mutant
    • Azevedo, R. A., Arana, J. L., Arruda, P. (1990). Biochemical genetics of the interaction of the lysine plus threonine resistant mutant Ltr*19 with opaque-2 maize mutant. Plant Sci. 70:81-90.
    • (1990) Plant Sci. , vol.70 , pp. 81-90
    • Azevedo, R.A.1    Arana, J.L.2    Arruda, P.3
  • 5
    • 0031260404 scopus 로고    scopus 로고
    • The biosynthesis and metabolism of the aspartate derived amino acids in higher plants
    • Azevedo, R. A., Arruda, P., Turner, W. L., Lea, P. J. (1997). The biosynthesis and metabolism of the aspartate derived amino acids in higher plants. Phytochemistry 46:395-419.
    • (1997) Phytochemistry , vol.46 , pp. 395-419
    • Azevedo, R.A.1    Arruda, P.2    Turner, W.L.3    Lea, P.J.4
  • 9
    • 0032245851 scopus 로고    scopus 로고
    • Improvement of energy, amino acid digestibility and growth performance by supplementing microbial enzymes to hulless barley diets for pigs
    • Baidoo, S. K., Liu, Y. G., Yungblut, D. (1997). Improvement of energy, amino acid digestibility and growth performance by supplementing microbial enzymes to hulless barley diets for pigs. Can. J. Anim. Sci. 78:625-631.
    • (1997) Can. J. Anim. Sci. , vol.78 , pp. 625-631
    • Baidoo, S.K.1    Liu, Y.G.2    Yungblut, D.3
  • 10
    • 0032871713 scopus 로고    scopus 로고
    • The potential of hull-less barley
    • Bhatty, R. S. (1999). The potential of hull-less barley. Cereal Chem. 76:589-599.
    • (1999) Cereal Chem. , vol.76 , pp. 589-599
    • Bhatty, R.S.1
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0013968749 scopus 로고
    • Separation and estimation of amino acids in crude plant extracts by thin-layer electrophoresis and chromatography
    • Bieleski, R. L., Turner, N. A. (1966). Separation and estimation of amino acids in crude plant extracts by thin-layer electrophoresis and chromatography. Anal. Biochem. 17:278-293.
    • (1966) Anal. Biochem. , vol.17 , pp. 278-293
    • Bieleski, R.L.1    Turner, N.A.2
  • 13
    • 1842713088 scopus 로고    scopus 로고
    • Biotechnology of wine yeast
    • Bison, L. F. (2004). Biotechnology of wine yeast. Food Biotechnol. 18:63-96.
    • (2004) Food Biotechnol. , vol.18 , pp. 63-96
    • Bison, L.F.1
  • 14
    • 84988074679 scopus 로고
    • Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., Gross, H. J. (1987). Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 15
    • 0029186792 scopus 로고
    • Protein content and composition in crosses between wild and cultivated barley
    • Corke, H. (1995). Protein content and composition in crosses between wild and cultivated barley. Cereal Res. Commun. 23:411-417.
    • (1995) Cereal Res. Commun. , vol.23 , pp. 411-417
    • Corke, H.1
  • 16
    • 0033893560 scopus 로고    scopus 로고
    • Hordein variation in Brazilian barley varieties (Hordeum vulgare L.) and wild barley (H. euclaston Steud. and H. stenostachys Godr.)
    • Echart-Almeida, C., Cavalli-Molina, S. (2000). Hordein variation in Brazilian barley varieties (Hordeum vulgare L.) and wild barley (H. euclaston Steud. and H. stenostachys Godr.). Genet. Mol. Biol. 23:425-433.
    • (2000) Genet. Mol. Biol. , vol.23 , pp. 425-433
    • Echart-Almeida, C.1    Cavalli-Molina, S.2
  • 17
    • 0035609335 scopus 로고    scopus 로고
    • Hordein polypeptide patterns in relation to malting quality in Brazilian barley varieties
    • Echart-Almeida, C., Cavalli-Molina, S. (2001). Hordein polypeptide patterns in relation to malting quality in Brazilian barley varieties. Pesq. Agropec. Bras. 36:1-11.
    • (2001) Pesq. Agropec. Bras. , vol.36 , pp. 1-11
    • Echart-Almeida, C.1    Cavalli-Molina, S.2
  • 18
    • 84988158460 scopus 로고
    • Nutrient composition of the hull-less barley variety, Condor
    • Edney, M. J., Tkachuk, R., MacGregor, A. W. (1992). Nutrient composition of the hull-less barley variety, Condor. J. Sci. Food Agric. 60:451-456.
    • (1992) J. Sci. Food Agric. , vol.60 , pp. 451-456
    • Edney, M.J.1    Tkachuk, R.2    MacGregor, A.W.3
  • 19
    • 9944220797 scopus 로고
    • Amino acid composition of total protein and electrophoretic behavior of protein fractions of barley
    • El-Negoumy, A. M., Newman, C. W., Moss, B. R. (1979). Amino acid composition of total protein and electrophoretic behavior of protein fractions of barley. Cereal Chem. 56:468-473.
    • (1979) Cereal Chem. , vol.56 , pp. 468-473
    • El-Negoumy, A.M.1    Newman, C.W.2    Moss, B.R.3
  • 21
    • 9944266040 scopus 로고    scopus 로고
    • FAO.FAOSTAT Agriculture Data
    • FAO.FAOSTAT Agriculture Data. http://www.Fao.org/page/collections?subset = agriculture.
  • 22
    • 0034780387 scopus 로고    scopus 로고
    • Study of metallopeptidase isozymes from malted barley (Hordeum vulgare cv. Morex)
    • Fontanini, D., Jones, B. L. (2001). Study of metallopeptidase isozymes from malted barley (Hordeum vulgare cv. Morex). J. Agric. Food Chem. 49:4903-4911.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4903-4911
    • Fontanini, D.1    Jones, B.L.2
  • 23
    • 0030758692 scopus 로고    scopus 로고
    • The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypeptide
    • Gaziola, S. A., Teixeira, C. M. G., Lugli, J., Sodek, L., Azevedo, R. A. (1997). The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypeptide. Eur. J. Biochem. 247:364-371.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 364-371
    • Gaziola, S.A.1    Teixeira, C.M.G.2    Lugli, J.3    Sodek, L.4    Azevedo, R.A.5
  • 25
    • 0035164832 scopus 로고    scopus 로고
    • Biochemical, genetic, and molecular characterization of wheat endosperm proteins
    • Gianibelli, M. C., Larroque, O. R., MacRitchie, F., Wrigley, C. W. (2001). Biochemical, genetic, and molecular characterization of wheat endosperm proteins. Cereal Chem. 78:635-646.
    • (2001) Cereal Chem. , vol.78 , pp. 635-646
    • Gianibelli, M.C.1    Larroque, O.R.2    MacRitchie, F.3    Wrigley, C.W.4
  • 26
    • 0037626984 scopus 로고    scopus 로고
    • Integrated plant proteomics - Putting the green genomes to work
    • Heazlewood, J. L., Harvey Millar, A. (2003). Integrated plant proteomics - putting the green genomes to work. Funct. Plant Biol. 30:471-482.
    • (2003) Funct. Plant Biol. , vol.30 , pp. 471-482
    • Heazlewood, J.L.1    Harvey Millar, A.2
  • 27
    • 0038268705 scopus 로고    scopus 로고
    • Molecular aspects of methionine biosynthesis
    • Hesse, H., Hoefgen, R. (2003). Molecular aspects of methionine biosynthesis. Trends Plant Sci. 8:259-262.
    • (2003) Trends Plant Sci. , vol.8 , pp. 259-262
    • Hesse, H.1    Hoefgen, R.2
  • 28
    • 0345504761 scopus 로고    scopus 로고
    • The role of opaque-2 in the control of lysine-degrading activities in developing maize endosperm
    • Kemper, E. L., Cord-Neto, G., Papes, F., Martinez-Moraes, K. C., Leite, A., Arruda, P. (1999). The role of opaque-2 in the control of lysine-degrading activities in developing maize endosperm. Plant Cell 11:1981-1994.
    • (1999) Plant Cell , vol.11 , pp. 1981-1994
    • Kemper, E.L.1    Cord-Neto, G.2    Papes, F.3    Martinez-Moraes, K.C.4    Leite, A.5    Arruda, P.6
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T 4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T 4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0033800110 scopus 로고    scopus 로고
    • Improved method for isolation and quantification α-amino nitrogen as nonprotein, true protein, salt-soluble proteins, zeins, and true glutelins in maize endosperm
    • Landry, J., Delhaye, S., Damerval, C. (2000). Improved method for isolation and quantification α-amino nitrogen as nonprotein, true protein, salt-soluble proteins, zeins, and true glutelins in maize endosperm. Cereal Chem. 77:620-626.
    • (2000) Cereal Chem. , vol.77 , pp. 620-626
    • Landry, J.1    Delhaye, S.2    Damerval, C.3
  • 31
    • 0142152837 scopus 로고
    • Barley proteins
    • Lásztity, R., ed. Boca Raton, Florida: CRC Press
    • Lásztity, R. (1984). Barley proteins. In: Lásztity, R., ed. The Chemistry of Cereal Proteins. Boca Raton, Florida: CRC Press, pp. 117-130.
    • (1984) The Chemistry of Cereal Proteins , pp. 117-130
    • Lásztity, R.1
  • 33
    • 1842663046 scopus 로고    scopus 로고
    • The application of real-time PCR to food and agricultural systems. A review
    • Levin, R. E. (2004). The application of real-time PCR to food and agricultural systems. A review. Food Biotechnol. 18:97-133.
    • (2004) Food Biotechnol. , vol.18 , pp. 97-133
    • Levin, R.E.1
  • 34
    • 0346829881 scopus 로고    scopus 로고
    • Improved procedures for extraction of lysine 2-oxoglutarate reductase/saccharopine dehydrogenase (LOR/SDH) enzyme from Phaseolus vulgaris cultivars
    • Lima, S. T. C., Azevedo, R. A., Santoro, L. G. (2003a). Improved procedures for extraction of lysine 2-oxoglutarate reductase/saccharopine dehydrogenase (LOR/SDH) enzyme from Phaseolus vulgaris cultivars. New Zeal. J. Crop. Hort. Sci. 31:261-268.
    • (2003) New Zeal. J. Crop. Hort. Sci. , vol.31 , pp. 261-268
    • Lima, S.T.C.1    Azevedo, R.A.2    Santoro, L.G.3
  • 35
    • 12444280061 scopus 로고    scopus 로고
    • Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris
    • Lima, S. T. C., Azevedo, R. A., Santoro, L. G., Gaziola, S. A., Lea, P. J. (2003b). Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris. Amino Acids 24:179-186.
    • (2003) Amino Acids , vol.24 , pp. 179-186
    • Lima, S.T.C.1    Azevedo, R.A.2    Santoro, L.G.3    Gaziola, S.A.4    Lea, P.J.5
  • 36
    • 0002338533 scopus 로고
    • Protein composition of a high-protein barley flour and barley grain
    • Linko, R., Lapveteläinen, A., Laakso, P., Kallio, H. (1989). Protein composition of a high-protein barley flour and barley grain. Cereal Chem. 66:478-482.
    • (1989) Cereal Chem. , vol.66 , pp. 478-482
    • Linko, R.1    Lapveteläinen, A.2    Laakso, P.3    Kallio, H.4
  • 37
    • 1442314010 scopus 로고    scopus 로고
    • The influence of nitrogen supply on antioxidant enzymes in plant roots
    • Medici, L. O., Azevedo, R. A., Smith, R. J., Lea, P. J. (2004). The influence of nitrogen supply on antioxidant enzymes in plant roots. Funct. Plant Biol. 31:1-9.
    • (2004) Funct. Plant Biol. , vol.31 , pp. 1-9
    • Medici, L.O.1    Azevedo, R.A.2    Smith, R.J.3    Lea, P.J.4
  • 40
    • 0002699477 scopus 로고
    • Nutritive properties of proteins of the maize kernel
    • Osborne, T. B., Mendel, L. B. (1914). Nutritive properties of proteins of the maize kernel. J. Biol. Chem. 18:1-6.
    • (1914) J. Biol. Chem. , vol.18 , pp. 1-6
    • Osborne, T.B.1    Mendel, L.B.2
  • 41
  • 42
    • 84985316857 scopus 로고
    • Fractionation and amino acid analysis of the salt-soluble protein fraction of normal and high lysine barleys
    • Rhodes, A. P., Gill, A. A. (1980). Fractionation and amino acid analysis of the salt-soluble protein fraction of normal and high lysine barleys. J. Sci. Food Agric. 31:467-473.
    • (1980) J. Sci. Food Agric. , vol.31 , pp. 467-473
    • Rhodes, A.P.1    Gill, A.A.2
  • 45
    • 0002427947 scopus 로고
    • Barley seed protein
    • MacGregor, A. W., Bhatty, R. S., eds. St. Paul, MN: American Association of Cereal Chemists
    • Shewry, P. R. (1993). Barley seed protein. In: MacGregor, A. W., Bhatty, R. S., eds. Barley: Chemistry and Technology. St. Paul, MN: American Association of Cereal Chemists, pp. 131-197.
    • (1993) Barley: Chemistry and Technology , pp. 131-197
    • Shewry, P.R.1
  • 46
    • 84986790259 scopus 로고
    • A comparison of methods for the extraction and separation of hordein fractions from 29 barley varieties
    • Shewry, P. R., Ellis, R. S., Pratt, H. M., Miflin, B. J. (1978). A comparison of methods for the extraction and separation of hordein fractions from 29 barley varieties. J. Sci. Food Agric. 29:433-441.
    • (1978) J. Sci. Food Agric. , vol.29 , pp. 433-441
    • Shewry, P.R.1    Ellis, R.S.2    Pratt, H.M.3    Miflin, B.J.4
  • 47
    • 0018833713 scopus 로고
    • Effect of high-lysine mutations on the protein fractions of barley grain
    • Shewry, P. R., Faulks, A. J., Miflin, B. J. (1980). Effect of high-lysine mutations on the protein fractions of barley grain. Biochem. Genet. 18:133-151.
    • (1980) Biochem. Genet. , vol.18 , pp. 133-151
    • Shewry, P.R.1    Faulks, A.J.2    Miflin, B.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.