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Volumn 55, Issue 406, 2004, Pages 2241-2249

A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins

Author keywords

conglycinin; Legumain like proteinase; Papain like proteinase; Phaseolin; Proteolysis; Seed storage protein degradation

Indexed keywords

CROPS; DEGRADATION; ENZYME KINETICS; ENZYMES; HYDROLYSIS;

EID: 5144228267     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/erh247     Document Type: Article
Times cited : (39)

References (35)
  • 1
    • 5144234226 scopus 로고
    • Substrate specificity of sulfhydryl protease purified from germinating com
    • Abe M, Arai S, Fujimaki M. 1978. Substrate specificity of sulfhydryl protease purified from germinating com. Agricultural and Biological Chemistry 42, 1813-1819.
    • (1978) Agricultural and Biological Chemistry , vol.42 , pp. 1813-1819
    • Abe, M.1    Arai, S.2    Fujimaki, M.3
  • 2
    • 0032818557 scopus 로고    scopus 로고
    • Characterization of novel cysteine proteases from germinating cotyledons of soybean. [Glycine max (L.) Merrill]
    • Asano M, Suzuki S, Kawai M, Miwa T, Shibai H. 1999. Characterization of novel cysteine proteases from germinating cotyledons of soybean. [Glycine max (L.) Merrill]. Journal of Biochemistry (Tokyo) 126, 296-301.
    • (1999) Journal of Biochemistry (Tokyo) , vol.126 , pp. 296-301
    • Asano, M.1    Suzuki, S.2    Kawai, M.3    Miwa, T.4    Shibai, H.5
  • 3
    • 0017407885 scopus 로고
    • Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings
    • Baumgartner B, Chrispeels MJ. 1977. Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings. European Journal of Biochemistry 77, 223-233.
    • (1977) European Journal of Biochemistry , vol.77 , pp. 223-233
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 4
    • 0000434454 scopus 로고
    • Purification of an endopeptidase involved in storage protein degradation in Phaseolus vulgaris L. cotyledons
    • Boylan MT, Sussex IM. 1987. Purification of an endopeptidase involved in storage protein degradation in Phaseolus vulgaris L. cotyledons. Planta 170, 343-352.
    • (1987) Planta , vol.170 , pp. 343-352
    • Boylan, M.T.1    Sussex, I.M.2
  • 5
    • 0025269261 scopus 로고
    • Conformational characteristics of legume 7S globulins as revealed by circular dichroic, derivative UV absorption and fluorescence techniques
    • Desphande SS, Damodaran S. 1990. Conformational characteristics of legume 7S globulins as revealed by circular dichroic, derivative UV absorption and fluorescence techniques. International Journal of Peptide and Protein Research 35, 25-34.
    • (1990) International Journal of Peptide and Protein Research , vol.35 , pp. 25-34
    • Desphande, S.S.1    Damodaran, S.2
  • 6
    • 0033624194 scopus 로고    scopus 로고
    • The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: Developmental patterns, intracellular localization and functions in globulin proteolysis
    • Fischer J, Becker C, Hillmer S, Horstmann C, Neubohn B, Schlereth A, Senyuk VI, Shutov AD, Müntz K. 2000. The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: developmental patterns, intracellular localization and functions in globulin proteolysis. Plant Molecular Biology 43, 83-101.
    • (2000) Plant Molecular Biology , vol.43 , pp. 83-101
    • Fischer, J.1    Becker, C.2    Hillmer, S.3    Horstmann, C.4    Neubohn, B.5    Schlereth, A.6    Senyuk, V.I.7    Shutov, A.D.8    Müntz, K.9
  • 7
    • 0002709844 scopus 로고    scopus 로고
    • Swiss-PdbViewer: A fast and easy-to-use PDBViewer for Macintosh and PC
    • Guex N, Peitsch MC. 1996. Swiss-PdbViewer: a fast and easy-to-use PDBViewer for Macintosh and PC. Protein Data Bank Quarterly Newsletter 77, 7.
    • (1996) Protein Data Bank Quarterly Newsletter , vol.77 , pp. 7
    • Guex, N.1    Peitsch, M.C.2
  • 8
    • 0000129621 scopus 로고
    • Equal expression of the maternal and paternal alleles for polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris
    • Hall TC, McLeester RC, Bliss FA. 1977. Equal expression of the maternal and paternal alleles for polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris. Plant Physiology 59, 1122-1124.
    • (1977) Plant Physiology , vol.59 , pp. 1122-1124
    • Hall, T.C.1    McLeester, R.C.2    Bliss, F.A.3
  • 9
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays
    • Kembhavi AA, Buttle DJ, Knight CG, Barret AA. 1993. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. Archives of Biochemistry and Biophysics 303, 208-213.
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barret, A.A.4
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
    • Lawrence MC, Izard T, Beuchat M, Blagrove RJ, Colman PR. 1994. Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology 238, 748-776.
    • (1994) Journal of Molecular Biology , vol.238 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrove, R.J.4    Colman, P.R.5
  • 13
    • 0030151307 scopus 로고    scopus 로고
    • Purification, characterization and crystallization of single molecular species of beta-conglycinin from soybean seeds
    • Morita S, Fukase M, Yamaguchi M, Fukuda Y, Morita Y. 1996. Purification, characterization and crystallization of single molecular species of beta-conglycinin from soybean seeds. Bioscience, Biotechnology and Biochemistry 60, 866-873.
    • (1996) Bioscience, Biotechnology and Biochemistry , vol.60 , pp. 866-873
    • Morita, S.1    Fukase, M.2    Yamaguchi, M.3    Fukuda, Y.4    Morita, Y.5
  • 14
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Müntz K. 1996. Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. Journal of Experimental Botany 47, 605-622.
    • (1996) Journal of Experimental Botany , vol.47 , pp. 605-622
    • Müntz, K.1
  • 15
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Müntz K, Shutov AD. 2002. Legumains and their functions in plants. Trends in Plant Science 7, 340-344.
    • (2002) Trends in Plant Science , vol.7 , pp. 340-344
    • Müntz, K.1    Shutov, A.D.2
  • 16
    • 0029008688 scopus 로고
    • Purification of an processing enzyme (VmPE-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP)
    • Okamoto T, Minamikawa T. 1995. Purification of an processing enzyme (VmPE-1) that is involved in post-translational processing of a plant cysteine endopeptidase (SH-EP). European Journal of Biochemistry 231, 300-305.
    • (1995) European Journal of Biochemistry , vol.231 , pp. 300-305
    • Okamoto, T.1    Minamikawa, T.2
  • 21
    • 0035830722 scopus 로고    scopus 로고
    • Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean β-conglycinin seed proteins
    • Seo S, Tan-Wilson A, Wilson KA. 2000. Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean β-conglycinin seed proteins. Biochimica et Biophysica Acta 1545, 192-206.
    • (2000) Biochimica et Biophysica Acta , vol.1545 , pp. 192-206
    • Seo, S.1    Tan-Wilson, A.2    Wilson, K.A.3
  • 22
    • 0011317058 scopus 로고
    • Cysteine proteinase from germinated wheat seeds: Partial purification and hydrolysis of gluten
    • Shutov AD, Beltey NC, Vaintraub IA. 1984a. Cysteine proteinase from germinated wheat seeds: partial purification and hydrolysis of gluten. Biokhimya 49, 1171-1177.
    • (1984) Biokhimya , vol.49 , pp. 1171-1177
    • Shutov, A.D.1    Beltey, N.C.2    Vaintraub, I.A.3
  • 23
    • 0000207074 scopus 로고
    • Protease a from germinating vetch seeds: Purification by affinity chromatography and substrate specificity studies
    • Shutov AD, Bulmaga VP, Vaintraub IA. 1984b. Protease A from germinating vetch seeds: Purification by affinity chromatography and substrate specificity studies. Biochemie und Physiologie der Pflanzen 179, 191-196.
    • (1984) Biochemie und Physiologie der Pflanzen , vol.179 , pp. 191-196
    • Shutov, A.D.1    Bulmaga, V.P.2    Vaintraub, I.A.3
  • 24
    • 0019567099 scopus 로고
    • Study of modification of vetch storage proteins during germination and proteolysis
    • Shutov AD, Bulmaga VP, Boldt E, Vaintraub IA. 1981. Study of modification of vetch storage proteins during germination and proteolysis. Biokhimya 46, 841-850.
    • (1981) Biokhimya , vol.46 , pp. 841-850
    • Shutov, A.D.1    Bulmaga, V.P.2    Boldt, E.3    Vaintraub, I.A.4
  • 25
    • 0004483403 scopus 로고
    • Purification and partial characterization of proteinase B from germinating vetch seeds
    • English translation
    • Shutov AD, Lanh DN, Vaintraub IA. 1982. Purification and partial characterization of proteinase B from germinating vetch seeds (English translation). Biokhimya 47, 678-685.
    • (1982) Biokhimya , vol.47 , pp. 678-685
    • Shutov, A.D.1    Lanh, D.N.2    Vaintraub, I.A.3
  • 26
    • 0000024298 scopus 로고
    • Degradation of storage proteins in germinating seeds
    • Shutov AD, Vaintraub IA. 1987. Degradation of storage proteins in germinating seeds. Phytochemistry 26, 1557-1566.
    • (1987) Phytochemistry , vol.26 , pp. 1557-1566
    • Shutov, A.D.1    Vaintraub, I.A.2
  • 28
    • 0033919065 scopus 로고    scopus 로고
    • Different functions of vicilin and legumin are reflected in the histopattern of globulin mobilization during germination of vetch (Vicia sativa L.)
    • Tiedemann J, Neubohn B, Müntz K. 2000. Different functions of vicilin and legumin are reflected in the histopattern of globulin mobilization during germination of vetch (Vicia sativa L.). Planta 211, 1-12.
    • (2000) Planta , vol.211 , pp. 1-12
    • Tiedemann, J.1    Neubohn, B.2    Müntz, K.3
  • 29
    • 0035028591 scopus 로고    scopus 로고
    • Differential tissue-specific expression of cysteine proteinases forms the basis for the fine-tuned mobilization of storage globulin during and after germination in legume seeds
    • Tiedemann J, Schlereth A, Müntz K. 2001. Differential tissue-specific expression of cysteine proteinases forms the basis for the fine-tuned mobilization of storage globulin during and after germination in legume seeds. Planta 212, 728-738.
    • (2001) Planta , vol.212 , pp. 728-738
    • Tiedemann, J.1    Schlereth, A.2    Müntz, K.3
  • 30
    • 0142073622 scopus 로고    scopus 로고
    • Kinetics of co-operative proteolysis
    • Vaintraub IA. 1998. Kinetics of co-operative proteolysis. Nahrung 42, 59-60.
    • (1998) Nahrung , vol.42 , pp. 59-60
    • Vaintraub, I.A.1
  • 31
    • 0017151821 scopus 로고
    • The action of trypsin and chymotrypsin on the storage proteins of some leguminous seeds
    • Vaintraub IA, Bassüner R, Shutov AD. 1976. The action of trypsin and chymotrypsin on the storage proteins of some leguminous seeds. Nahrung 20, 763-771.
    • (1976) Nahrung , vol.20 , pp. 763-771
    • Vaintraub, I.A.1    Bassüner, R.2    Shutov, A.D.3
  • 32
    • 0342578250 scopus 로고
    • Cysteine proteinase from germinating sunflower seeds: Partial purification and effect on the storage 11S protein
    • Vaintraub IA, Ropot ES. 1988. Cysteine proteinase from germinating sunflower seeds: partial purification and effect on the storage 11S protein. Biokhimya 53, 776-780.
    • (1988) Biokhimya , vol.53 , pp. 776-780
    • Vaintraub, I.A.1    Ropot, E.S.2
  • 33
    • 84982614583 scopus 로고
    • The action of pepsin on the storage proteins of some leguminous seeds
    • Vaintraub IA, Seliger P, Shutov AD. 1979. The action of pepsin on the storage proteins of some leguminous seeds. Nahrung 23, 15-21.
    • (1979) Nahrung , vol.23 , pp. 15-21
    • Vaintraub, I.A.1    Seliger, P.2    Shutov, A.D.3
  • 35
    • 0002150829 scopus 로고
    • Role of proteolytic enzymes in the mobilization of protein reserves in germinating dicot seeds
    • Dalling MJ, ed. Boca Raton, Florida: CRC Press Inc.
    • Wilson KA. 1986. Role of proteolytic enzymes in the mobilization of protein reserves in germinating dicot seeds. In: Dalling MJ, ed. Plant proteolytic enzymes. Vol. II. Boca Raton, Florida: CRC Press Inc., 19-47.
    • (1986) Plant Proteolytic Enzymes , vol.2 , pp. 19-47
    • Wilson, K.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.