메뉴 건너뛰기




Volumn 47, Issue 298, 1996, Pages 605-622

Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds

Author keywords

Dicotyledons; Proteases; Proteolytic cleavage; Seeds; Storage proteins

Indexed keywords

DICOTYLEDONEAE;

EID: 0001064980     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/47.5.605     Document Type: Review
Times cited : (134)

References (120)
  • 1
    • 0027477474 scopus 로고
    • Asparaginyl endopeptidases of jack bean seeds. Purification, characterization, and high utility in protein sequence analysis
    • Abe Y, Shirane K, Yokosawa H, Matsushita H, Mitta M, Kato I, Ishii S. 1993. Asparaginyl endopeptidases of jack bean seeds. Purification, characterization, and high utility in protein sequence analysis. Journal of Biological Chemistry 268, 3525-9.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 3525-3529
    • Abe, Y.1    Shirane, K.2    Yokosawa, H.3    Matsushita, H.4    Mitta, M.5    Kato, I.6    Ishii, S.7
  • 2
    • 0000812569 scopus 로고
    • Origin and development of protein bodies in cotyledons of Vicia faba
    • Adler K, Müntz K. 1983. Origin and development of protein bodies in cotyledons of Vicia faba. Planta 157, 401-10.
    • (1983) Planta , vol.157 , pp. 401-410
    • Adler, K.1    Müntz, K.2
  • 3
    • 0025317953 scopus 로고
    • Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP)
    • Akasofu H, Yamauchi D, Minamikawa T. 1990. Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP). Nucleic Acids Research 18, 1892.
    • (1990) Nucleic Acids Research , vol.18 , pp. 1892
    • Akasofu, H.1    Yamauchi, D.2    Minamikawa, T.3
  • 4
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds
    • Akasofu H, Yamauchi D, Mitsuhashi W, Minamikawa T. 1989. Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Research 17, 6733.
    • (1989) Nucleic Acids Research , vol.17 , pp. 6733
    • Akasofu, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 5
    • 5844416089 scopus 로고
    • Effects of leupeptin on proteinase and germination of castor beans
    • Alpi A, Beevers H. 1981. Effects of leupeptin on proteinase and germination of castor beans. Plant Physiology 68, 851-3.
    • (1981) Plant Physiology , vol.68 , pp. 851-853
    • Alpi, A.1    Beevers, H.2
  • 8
    • 0003029728 scopus 로고
    • The development of proteolytic activity and protein degradation during the germination of Pisum sativum L.
    • Berl.
    • Basha SMM, Beevers L. 1975. The development of proteolytic activity and protein degradation during the germination of Pisum sativum L. Planta (Berl.) 124, 77-87.
    • (1975) Planta , vol.124 , pp. 77-87
    • Basha, S.M.M.1    Beevers, L.2
  • 9
    • 0023665356 scopus 로고
    • The primary structure of the predominating vicilin storage protein subunit from field bean seeds (Vicia faba L. var. minor cv. Fribo)
    • Bassüncr R, Nong VH, Jung R, Saalbach G, Müntz K. 1987. The primary structure of the predominating vicilin storage protein subunit from field bean seeds (Vicia faba L. var. minor cv. Fribo). Nucleic Acids Research 15, 9609.
    • (1987) Nucleic Acids Research , vol.15 , pp. 9609
    • Bassüncr, R.1    Nong, V.H.2    Jung, R.3    Saalbach, G.4    Müntz, K.5
  • 10
    • 0021773265 scopus 로고
    • Signal recognition particle triggers the translation of storage globulin polypeptides from field bean (Vicia faba L.) across mammalian endoplasmic reticulum membrane
    • Bassüner R, Wobus U, Rapoport TA. 1984. Signal recognition particle triggers the translation of storage globulin polypeptides from field bean (Vicia faba L.) across mammalian endoplasmic reticulum membrane. FEBS Letters 166, 314-20.
    • (1984) FEBS Letters , vol.166 , pp. 314-320
    • Bassüner, R.1    Wobus, U.2    Rapoport, T.A.3
  • 11
    • 0002295661 scopus 로고
    • Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung beans
    • Baumgartner B, Chrispeels MJ. 1976. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung beans. Plant Physiology 58, 1-6.
    • (1976) Plant Physiology , vol.58 , pp. 1-6
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 12
    • 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, 223-33.
    • (1977) European Journal of Biochemistry , vol.77 , pp. 223-233
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 14
    • 0018091598 scopus 로고
    • Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy
    • Baumgartner B, Tokuyasu KT, Chrispeels MJ. 1978. Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy. Journal of Cell Biology 79, 10-19.
    • (1978) Journal of Cell Biology , vol.79 , pp. 10-19
    • Baumgartner, B.1    Tokuyasu, K.T.2    Chrispeels, M.J.3
  • 15
    • 0028535314 scopus 로고
    • PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L.
    • Becker C, Fischer J, Nong VH, Müntz K. 1994. PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L. Plant Molecular Biology 26, 1207-12.
    • (1994) Plant Molecular Biology , vol.26 , pp. 1207-1212
    • Becker, C.1    Fischer, J.2    Nong, V.H.3    Müntz, K.4
  • 18
    • 0025678423 scopus 로고
    • Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds
    • Belozersky MA, Dunaevsky YE, Voskoboynikova E. 1990. Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds. Biochemical Journal 272, 677-82.
    • (1990) Biochemical Journal , vol.272 , pp. 677-682
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Voskoboynikova, E.3
  • 20
    • 0000255424 scopus 로고
    • Characterization of soybean endopeptidase activity using exogenous and endogenous substrates
    • Bond HM, Bowles DJ. 1983. Characterization of soybean endopeptidase activity using exogenous and endogenous substrates. Plant Physiology 72, 345-50.
    • (1983) Plant Physiology , vol.72 , pp. 345-350
    • Bond, H.M.1    Bowles, D.J.2
  • 22
    • 0000434454 scopus 로고
    • Purification of an endopeptidase involved with storage-protein degradation in Phaseolus vulgaris L. cotyledons
    • Boylan MT, Sussex IM. 1987. Purification of an endopeptidase involved with storage-protein degradation in Phaseolus vulgaris L. cotyledons. Planta 170, 343-52.
    • (1987) Planta , vol.170 , pp. 343-352
    • Boylan, M.T.1    Sussex, I.M.2
  • 23
    • 0022001083 scopus 로고
    • Polypeptide ligation occurs during post-translational modification of concanavalin A
    • Carrington DM, Auffret A, Hanke DE. 1984. Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature 313, 64-7.
    • (1984) Nature , vol.313 , pp. 64-67
    • Carrington, D.M.1    Auffret, A.2    Hanke, D.E.3
  • 24
    • 0000720759 scopus 로고
    • Developmental biochemistry of cotton seed embryogenesis and germination. XVIII. cDNA and amino acid sequences of members of the storage protein families
    • Chlan CA, Pyle JB, Legocki AB, Dure III L. 1986. Developmental biochemistry of cotton seed embryogenesis and germination. XVIII. cDNA and amino acid sequences of members of the storage protein families. Plant Molecular Biology 7, 475-89.
    • (1986) Plant Molecular Biology , vol.7 , pp. 475-489
    • Chlan, C.A.1    Pyle, J.B.2    Legocki, A.B.3    Dure III, L.4
  • 25
    • 0000149283 scopus 로고
    • Developmental biochemistry of cottonseed embryogenesis and germination. XIX. Sequences and genomic organization of the α-globulin (vicilin) genes of cottonseed
    • Chlan CA, Borroto K, Kamalay JA, Dure III L. 1987. Developmental biochemistry of cottonseed embryogenesis and germination. XIX. Sequences and genomic organization of the α-globulin (vicilin) genes of cottonseed. Plant Molecular Biology 9, 533-46.
    • (1987) Plant Molecular Biology , vol.9 , pp. 533-546
    • Chlan, C.A.1    Borroto, K.2    Kamalay, J.A.3    Dure III, L.4
  • 26
  • 27
    • 0842345853 scopus 로고
    • Trypsin inhibitor in mung bean cotyledons. Purification, characteristics, subcellular localization, and metabolism
    • Chrispeels MJ, Baumgartner B. 1978. Trypsin inhibitor in mung bean cotyledons. Purification, characteristics, subcellular localization, and metabolism. Plant Physiology 61, 617-23.
    • (1978) Plant Physiology , vol.61 , pp. 617-623
    • Chrispeels, M.J.1    Baumgartner, B.2
  • 28
    • 0001743127 scopus 로고
    • Control of storage protein metabolism in the cotyledons of germinating mung beans: Role of endopeptidase
    • Chrispeels MJ, Boulter D. 1975. Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase. Plant Physiology 55, 1031-7.
    • (1975) Plant Physiology , vol.55 , pp. 1031-1037
    • Chrispeels, M.J.1    Boulter, D.2
  • 29
    • 0026532891 scopus 로고
    • Short peptide domains target proteins to plant vacuoles
    • Chrispeels MJ, Raikhel NV. 1992. Short peptide domains target proteins to plant vacuoles. Cell 68, 613-16.
    • (1992) Cell , vol.68 , pp. 613-616
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 31
    • 0020132174 scopus 로고
    • Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons
    • Chrispeels MJ, Higgins TJV, Spencer D. 1982. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. Journal of Cell Biology 93, 306-13.
    • (1982) Journal of Cell Biology , vol.93 , pp. 306-313
    • Chrispeels, M.J.1    Higgins, T.J.V.2    Spencer, D.3
  • 32
    • 0028007714 scopus 로고
    • Characterization of asparaginyl endopeptidase activity in endosperm of developing and germinating castor oil seeds
    • Cornel FA, Plaxton WC. 1994. Characterization of asparaginyl endopeptidase activity in endosperm of developing and germinating castor oil seeds. Physiologia Plantarum 91, 599-604.
    • (1994) Physiologia Plantarum , vol.91 , pp. 599-604
    • Cornel, F.A.1    Plaxton, W.C.2
  • 33
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes - A new protease family
    • Dalbey RE, Heijne G von. 1992. Signal peptidases in prokaryotes and eukaryotes - a new protease family. Trends in Biochemical Sciences 17, 474-8.
    • (1992) Trends in Biochemical Sciences , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 35
    • 38249000222 scopus 로고
    • Immunocytochemical analysis of proteolysis in germinating soybean
    • Diaz P, Wilson KA, Tan-Wilson AL. 1993. Immunocytochemical analysis of proteolysis in germinating soybean. Phytochemistry 33, 961-8.
    • (1993) Phytochemistry , vol.33 , pp. 961-968
    • Diaz, P.1    Wilson, K.A.2    Tan-Wilson, A.L.3
  • 38
    • 0022977063 scopus 로고
    • The glycosylated seed storage proteins of Glycine max, Phaseolus and Phaseolus vulgaris: Structural homologies of genes and proteins
    • Doyle JJ, Schuler MA, Godette WD, Zenger V, Beachy R. 1986. The glycosylated seed storage proteins of Glycine max, Phaseolus and Phaseolus vulgaris: structural homologies of genes and proteins. Journal of Biological Chemistry 261, 9228-38.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 9228-9238
    • Doyle, J.J.1    Schuler, M.A.2    Godette, W.D.3    Zenger, V.4    Beachy, R.5
  • 39
    • 84989741845 scopus 로고
    • Proteolysis of the main storage protein of buckwheat seeds at the early stage of germination
    • Dunaevsky YE, Belozersky MA. 1989a. Proteolysis of the main storage protein of buckwheat seeds at the early stage of germination. Physiology Plantarum 75, 424-8.
    • (1989) Physiology Plantarum , vol.75 , pp. 424-428
    • Dunaevsky, Y.E.1    Belozersky, M.A.2
  • 40
    • 0000354436 scopus 로고
    • The role of cysteine proteinase and carboxypeptidase in the breakdown of storage proteins in buckwheat seeds
    • Dunaevsky YE, Belozersky MA. 1989b. The role of cysteine proteinase and carboxypeptidase in the breakdown of storage proteins in buckwheat seeds. Planta 179, 316-22.
    • (1989) Planta , vol.179 , pp. 316-322
    • Dunaevsky, Y.E.1    Belozersky, M.A.2
  • 41
    • 84989692644 scopus 로고
    • Effects of the embryonic axis and phytohormones on proteolysis of the storage protein in buckwheat seed
    • Dunaevsky YE, Belozersky MA. 1993. Effects of the embryonic axis and phytohormones on proteolysis of the storage protein in buckwheat seed. Physiologia Plantarum 88, 60-4.
    • (1993) Physiologia Plantarum , vol.88 , pp. 60-64
    • Dunaevsky, Y.E.1    Belozersky, M.A.2
  • 42
    • 0000867883 scopus 로고
    • Developmental biochemistry of cotton seed embryogenesis and germination. XII. Purification and properties of principal storage proteins
    • Dure III L, Chlan C. 1981. Developmental biochemistry of cotton seed embryogenesis and germination. XII. Purification and properties of principal storage proteins. Plant Physiology 68, 180-6.
    • (1981) Plant Physiology , vol.68 , pp. 180-186
    • Dure III, L.1    Chlan, C.2
  • 43
    • 0001872610 scopus 로고
    • Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds
    • Elpidina EN, Voskoboynikova NE, Belozersky MA, Dunaevsky YE. 1991. Localization of a metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds. Planta 185, 46-52.
    • (1991) Planta , vol.185 , pp. 46-52
    • Elpidina, E.N.1    Voskoboynikova, N.E.2    Belozersky, M.A.3    Dunaevsky, Y.E.4
  • 44
    • 0001142403 scopus 로고
    • Transport and processing of the glycosylated precursor of Concanavalin A in jack-bean
    • Faye L, Chrispeels MJ. 1987. Transport and processing of the glycosylated precursor of Concanavalin A in jack-bean. Planta 170, 217-24.
    • (1987) Planta , vol.170 , pp. 217-224
    • Faye, L.1    Chrispeels, M.J.2
  • 47
    • 0020396857 scopus 로고
    • The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.)
    • Gatehouse JA, Lycett GW, Croy RRD, Boulter D. 1982. The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.). Biochemical Journal 207, 629-32.
    • (1982) Biochemical Journal , vol.207 , pp. 629-632
    • Gatehouse, J.A.1    Lycett, G.W.2    Croy, R.R.D.3    Boulter, D.4
  • 48
    • 0021104094 scopus 로고
    • Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.)
    • Gatehouse JA, Lycett GW, Delauney AJ, Croy RRD, Boulter D. 1983. Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.). Biochemical Journal 212, 427-32.
    • (1983) Biochemical Journal , vol.212 , pp. 427-432
    • Gatehouse, J.A.1    Lycett, G.W.2    Delauney, A.J.3    Croy, R.R.D.4    Boulter, D.5
  • 49
    • 1842326229 scopus 로고
    • Control by the embryo axis of the breakdown of storage proteins in the endosperm of germinated castor bean seed: A role for gibberellic acid
    • Gifford DJ, Thakore E, Bewley JD. 1984. Control by the embryo axis of the breakdown of storage proteins in the endosperm of germinated castor bean seed: a role for gibberellic acid. Journal of Experimental Botany 35, 669-77.
    • (1984) Journal of Experimental Botany , vol.35 , pp. 669-677
    • Gifford, D.J.1    Thakore, E.2    Bewley, J.D.3
  • 50
    • 0025463350 scopus 로고
    • Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes
    • Guerrero FD, Jones JT, Mullet JE. 1990. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes. Plant Molecular Biology 15, 11-26.
    • (1990) Plant Molecular Biology , vol.15 , pp. 11-26
    • Guerrero, F.D.1    Jones, J.T.2    Mullet, J.E.3
  • 51
    • 0000235299 scopus 로고
    • Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons
    • Hara-Nishimura I, Nishimura M. 1987. Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons. Plant Physiology 85, 440-5.
    • (1987) Plant Physiology , vol.85 , pp. 440-445
    • Hara-Nishimura, I.1    Nishimura, M.2
  • 52
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura I, Inoue K, Nishimura M. 1991. A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Letters 294, 89-93.
    • (1991) FEBS Letters , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 54
    • 0027688051 scopus 로고
    • Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • Hara-Nishimura I, Takeuchi Y, Nishimura M. 1993a. Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. The Plant Cell 5, 1651-9.
    • (1993) The Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 55
    • 0027692821 scopus 로고
    • Vesicle transport and processing of the precursor to 2S albumin in pumpkin
    • Hara-Nishimura I, Takeuchi Y, Inoue K, Nishimura M. 1993b. Vesicle transport and processing of the precursor to 2S albumin in pumpkin. The Plant Journal 4, 793-800.
    • (1993) The Plant Journal , vol.4 , pp. 793-800
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Inoue, K.3    Nishimura, M.4
  • 56
    • 0000697061 scopus 로고
    • In vitro endoproteolytic cleavage of castor bean lectin precursor
    • Harley SM, Lord JM. 1985. In vitro endoproteolytic cleavage of castor bean lectin precursor. Plant Science 41, 111-16.
    • (1985) Plant Science , vol.41 , pp. 111-116
    • Harley, S.M.1    Lord, J.M.2
  • 57
    • 0001447022 scopus 로고
    • Histochemical and biochemical observations on storage protein metabolism and protein body autolysis in cotyledons of germinating mung beans
    • Harris N, Chrispeels MJ. 1975. Histochemical and biochemical observations on storage protein metabolism and protein body autolysis in cotyledons of germinating mung beans. Plant Physiology 56, 292-9.
    • (1975) Plant Physiology , vol.56 , pp. 292-299
    • Harris, N.1    Chrispeels, M.J.2
  • 58
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Heijne G von. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Research 14, 4683-90.
    • (1986) Nucleic Acids Research , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 59
    • 0028406309 scopus 로고
    • The legumin gene family: A reconstructed Vicia faba legumin gene encoding a high-molecular weight subunit is related to type B genes
    • Heim U, Baümlein H, Wobus U. 1994. The legumin gene family: a reconstructed Vicia faba legumin gene encoding a high-molecular weight subunit is related to type B genes. Plant Molecular Biology 25, 131-5.
    • (1994) Plant Molecular Biology , vol.25 , pp. 131-135
    • Heim, U.1    Baümlein, H.2    Wobus, U.3
  • 60
    • 0024894692 scopus 로고
    • The legumin gene family: Structure and evolutionary implication of Vicia faba B-type genes and pseudogenes
    • Heim U, Schubert R, Bäumlein H, Wobus U. 1989. The legumin gene family: structure and evolutionary implication of Vicia faba B-type genes and pseudogenes. Plant Molecular Biology 13, 653-63.
    • (1989) Plant Molecular Biology , vol.13 , pp. 653-663
    • Heim, U.1    Schubert, R.2    Bäumlein, H.3    Wobus, U.4
  • 61
    • 0000965330 scopus 로고
    • Apparent processing of a soybean oil body protein accompanies the onset of oil mobilization
    • Herman EM, Melroy DL, Buckout TJ. 1990. Apparent processing of a soybean oil body protein accompanies the onset of oil mobilization. Plant Physiology 94, 341-9.
    • (1990) Plant Physiology , vol.94 , pp. 341-349
    • Herman, E.M.1    Melroy, D.L.2    Buckout, T.J.3
  • 62
    • 0027139607 scopus 로고
    • A vacuolar processing enzyme in maturing and germinating seeds: Its distribution and associated changes during development
    • Hiraiwa N, Takeuchi Y, Nishimura M, Hara-Nishimura I. 1993. A vacuolar processing enzyme in maturing and germinating seeds: its distribution and associated changes during development. Plant Cell Physiology 34, 1197-204.
    • (1993) Plant Cell Physiology , vol.34 , pp. 1197-1204
    • Hiraiwa, N.1    Takeuchi, Y.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 63
    • 0028893601 scopus 로고
    • Protein storage vacuoles form de novo during pea cotyledon development
    • Hoh B, Hinz G, Jeong B-K, Robinson DG. 1995. Protein storage vacuoles form de novo during pea cotyledon development. Journal of Cell Science 108, 299-310.
    • (1995) Journal of Cell Science , vol.108 , pp. 299-310
    • Hoh, B.1    Hinz, G.2    Jeong, B.-K.3    Robinson, D.G.4
  • 64
    • 0039322123 scopus 로고
    • Polymorphism of legumin subunits from field bean (Vicia faba L. var. minor) and its relation to the corresponding multigene family
    • Horstmann C, Schlesier B, Otto A, Kostka S, Müntz K. 1993. Polymorphism of legumin subunits from field bean (Vicia faba L. var. minor) and its relation to the corresponding multigene family. Theoretical and Applied Genetics 86, 867-74.
    • (1993) Theoretical and Applied Genetics , vol.86 , pp. 867-874
    • Horstmann, C.1    Schlesier, B.2    Otto, A.3    Kostka, S.4    Müntz, K.5
  • 65
    • 0029240342 scopus 로고
    • Molecular characterization of proteins in protein-body membrane that disappear most rapidly during transformation of protein bodies into vacuoles
    • Inoue K, Motozaki A, Takeuchi Y, Nishimura M, Hara-Nishimura I. 1995. Molecular characterization of proteins in protein-body membrane that disappear most rapidly during transformation of protein bodies into vacuoles. The Plant Journal 7, 235-43.
    • (1995) The Plant Journal , vol.7 , pp. 235-243
    • Inoue, K.1    Motozaki, A.2    Takeuchi, Y.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 66
    • 0028673279 scopus 로고
    • Legumain: Asparaginyl endopeptidase
    • Ishii S-I. 1994. Legumain: asparaginyl endopeptidase. Methods in Enzymology 244, 604-15.
    • (1994) Methods in Enzymology , vol.244 , pp. 604-615
    • Ishii, S.-I.1
  • 67
    • 0000236658 scopus 로고
    • Site-specific limited proteolysis of legumin chloramphenicol acetyl transferase fusions in vitro and in transgenic tobacco seeds
    • Jung R, Saalbach G, Nielsen NC, Müntz K. 1993. Site-specific limited proteolysis of legumin chloramphenicol acetyl transferase fusions in vitro and in transgenic tobacco seeds. Journal of Experimental Botany 44, 343-9.
    • (1993) Journal of Experimental Botany , vol.44 , pp. 343-349
    • Jung, R.1    Saalbach, G.2    Nielsen, N.C.3    Müntz, K.4
  • 68
    • 0026625627 scopus 로고
    • A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation
    • Kalinski A, Melroy DL, Dwivedi RS, Herman EM. 1992. A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation. The Journal of Biological Chemistry 267, 12068-76.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 12068-12076
    • Kalinski, A.1    Melroy, D.L.2    Dwivedi, R.S.3    Herman, E.M.4
  • 69
    • 0025113503 scopus 로고
    • Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol protease of the papain family
    • Kalinski A, Weiseman JM, Matthews BF, Herman EM. 1990. Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol protease of the papain family. The Journal of Biological Chemistry 265, 13843-8.
    • (1990) The Journal of Biological Chemistry , vol.265 , pp. 13843-13848
    • Kalinski, A.1    Weiseman, J.M.2    Matthews, B.F.3    Herman, E.M.4
  • 70
    • 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, Barrett AJ. 1993. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. Archives of Biochemistry and Biophysics 303, 208-13.
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 71
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein in protein bodies of maize endosperm
    • Larkins BA, Hurkman WJ. 1978. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiology 62, 256-63.
    • (1978) Plant Physiology , vol.62 , pp. 256-263
    • Larkins, B.A.1    Hurkman, W.J.2
  • 72
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2.2 'Å resolution. Implication for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
    • Lawrence MC, Izard T, Beuchat M, Blagrove RJ, Colman PM. 1994. Structure of phaseolin at 2.2 'Å resolution. Implication for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology 238, 748-76.
    • (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.M.5
  • 76
    • 0028672745 scopus 로고
    • Eukaryotic microsomal signal peptidases
    • Barrett AJ, ed. San Diego: Academic Press, Inc.
    • Lively MO, Newsome AL, Nusier M. 1994. Eukaryotic microsomal signal peptidases. In: Barrett AJ, ed. Methods in enzymology. San Diego: Academic Press, Inc., 301-10.
    • (1994) Methods in Enzymology , pp. 301-310
    • Lively, M.O.1    Newsome, A.L.2    Nusier, M.3
  • 77
    • 0001076074 scopus 로고
    • Separation and characterization of two endopeptidases from cotyledons of germinating Vigna mungo seeds
    • Mitsuhashi W, Koshiba T, Minamikawa T. 1986. Separation and characterization of two endopeptidases from cotyledons of germinating Vigna mungo seeds. Plant Physiology 80, 628-34.
    • (1986) Plant Physiology , vol.80 , pp. 628-634
    • Mitsuhashi, W.1    Koshiba, T.2    Minamikawa, T.3
  • 78
    • 84897583639 scopus 로고
    • Synthesis and post-translational activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds
    • Mitsuhashi W, Minamikawa T. 1989. Synthesis and post-translational activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds. Plant Physiology 89, 274-9.
    • (1989) Plant Physiology , vol.89 , pp. 274-279
    • Mitsuhashi, W.1    Minamikawa, T.2
  • 79
    • 5844350359 scopus 로고
    • Storage and reactivation of high molecular nitrogen compounds in plants
    • Mohr H, Müntz K, eds. Nova Acta Leopoldina N.F.
    • Müntz K. 1994. Storage and reactivation of high molecular nitrogen compounds in plants. In: Mohr H, Müntz K, eds. The terrestrial nitrogen cycle as influenced by man. Nova Acta Leopoldina N.F. 288, 183-200.
    • (1994) The Terrestrial Nitrogen Cycle as Influenced by Man , vol.288 , pp. 183-200
    • Müntz, K.1
  • 80
    • 0002896996 scopus 로고
    • Proteolytic cleavage of storage proteins during embryogenesis and germination of legume seeds
    • Müntz K, Bassüner R, Lichtenfeld C, Scholz G, Weber E. 1985. Proteolytic cleavage of storage proteins during embryogenesis and germination of legume seeds. Physiologie Végétale 23, 75-94.
    • (1985) Physiologie Végétale , vol.23 , pp. 75-94
    • Müntz, K.1    Bassüner, R.2    Lichtenfeld, C.3    Scholz, G.4    Weber, E.5
  • 82
    • 0003754307 scopus 로고
    • Synthesis, processing, and targeting of legume seed proteins
    • Shewry PR, Stobart K, eds. Seed storage compounds, biosynthesis, interactions, and manipulation
    • Müntz K, Jung R, Saalbach G. 1993. Synthesis, processing, and targeting of legume seed proteins. In: Shewry PR, Stobart K, eds. Seed storage compounds, biosynthesis, interactions, and manipulation. Proceedings of the Phytochemical Society of Europe 5, 128-46.
    • (1993) Proceedings of the Phytochemical Society of Europe , vol.5 , pp. 128-146
    • Müntz, K.1    Jung, R.2    Saalbach, G.3
  • 83
    • 0027249370 scopus 로고
    • A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme
    • Muramatsu M, Fukazawa C. 1993. A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme. European Journal of Biochemistry 215, 123-32.
    • (1993) European Journal of Biochemistry , vol.215 , pp. 123-132
    • Muramatsu, M.1    Fukazawa, C.2
  • 84
    • 0029170467 scopus 로고
    • The influence of the embryonic axis and cytokinins on reserve mobilization in germinating lupin seeds
    • Nandi SK, Palni LMS, Klerk JM de. 1995. The influence of the embryonic axis and cytokinins on reserve mobilization in germinating lupin seeds. Journal of Experimental Botany 46, 329-36.
    • (1995) Journal of Experimental Botany , vol.46 , pp. 329-336
    • Nandi, S.K.1    Palni, L.M.S.2    De Klerk, J.M.3
  • 86
    • 0027552743 scopus 로고
    • Cloning, expression and crystallization of jack bean (Canavalia ensiformis) canavalin
    • Ng JD, Ko TP, McPherson A. 1993. Cloning, expression and crystallization of jack bean (Canavalia ensiformis) canavalin. Plant Physiology 101, 713-28.
    • (1993) Plant Physiology , vol.101 , pp. 713-728
    • Ng, J.D.1    Ko, T.P.2    McPherson, A.3
  • 88
    • 0001129084 scopus 로고
    • Degradation of the major storage protein of Phaseolus vulgaris during germination. Role of endogenous proteases and protease inhibitors
    • Nielsen SS, Liener IE. 1984. Degradation of the major storage protein of Phaseolus vulgaris during germination. Role of endogenous proteases and protease inhibitors. Plant Physiology 74, 494-8.
    • (1984) Plant Physiology , vol.74 , pp. 494-498
    • Nielsen, S.S.1    Liener, I.E.2
  • 89
    • 0028950917 scopus 로고
    • cDNA cloning for a putative cysteine proteinase from developing seeds of soybean
    • Nong VH, Becker C, Müntz K. 1995. cDNA cloning for a putative cysteine proteinase from developing seeds of soybean. Biochimica et Biophysica Acta 1261, 435-8.
    • (1995) Biochimica et Biophysica Acta , vol.1261 , pp. 435-438
    • Nong, V.H.1    Becker, C.2    Müntz, K.3
  • 90
    • 0028041312 scopus 로고
    • Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)
    • Okamoto T, Nakayama H, Seta K, Isobe T, Minamikawa T. 1994. Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP). FEBS Letters 351, 31-4.
    • (1994) FEBS Letters , vol.351 , pp. 31-34
    • Okamoto, T.1    Nakayama, H.2    Seta, K.3    Isobe, T.4    Minamikawa, T.5
  • 91
    • 0002399247 scopus 로고
    • The vegetable proteins
    • London: Longmans, Green & Co.
    • Osborne TB. 1924. The vegetable proteins. Monographs in biochemistry. London: Longmans, Green & Co.
    • (1924) Monographs in Biochemistry
    • Osborne, T.B.1
  • 92
    • 0001098671 scopus 로고
    • Characterization of the major protease involved in the soybean β-conglycinin storage protein metabolization
    • Qi, X, Wilson KA, Tan-Wilson AL. 1992. Characterization of the major protease involved in the soybean β-conglycinin storage protein metabolization. Plant Physiology 99, 725-33.
    • (1992) Plant Physiology , vol.99 , pp. 725-733
    • Qi, X.1    Wilson, K.A.2    Tan-Wilson, A.L.3
  • 93
    • 0028052666 scopus 로고
    • Characterization of a soybean β-conglycinin-degrading protease cleavage site
    • Qi X, Chen R, Wilson KA, Tan-Wilson AL. 1994. Characterization of a soybean β-conglycinin-degrading protease cleavage site. Plant Physiology 104, 127-33.
    • (1994) Plant Physiology , vol.104 , pp. 127-133
    • Qi, X.1    Chen, R.2    Wilson, K.A.3    Tan-Wilson, A.L.4
  • 95
    • 5844414149 scopus 로고
    • Multiple mechanism of protein body formation in pea cotyledons
    • in press
    • Robinson DG, Hinz G. 1995. Multiple mechanism of protein body formation in pea cotyledons. Plant Physiology and Biochemistry (in press).
    • (1995) Plant Physiology and Biochemistry
    • Robinson, D.G.1    Hinz, G.2
  • 96
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development?
    • Robinson DG, Hoh B, Hinz G, Jeong BK. 1995. One vacuole or two vacuoles: do protein storage vacuoles arise de novo during pea cotyledon development? Journal of Plant Physiology 145, 654-64.
    • (1995) Journal of Plant Physiology , vol.145 , pp. 654-664
    • Robinson, D.G.1    Hoh, B.2    Hinz, G.3    Jeong, B.K.4
  • 97
    • 0021103834 scopus 로고
    • Low molecular weight polypeptides of vicilin from Vicia faba L. are products of proteolytic breakdown
    • Scholz G, Manteuffel R, Müntz K, Rudolph A. 1983. Low molecular weight polypeptides of vicilin from Vicia faba L. are products of proteolytic breakdown. European Journal of Biochemistry 132, 103-7.
    • (1983) European Journal of Biochemistry , vol.132 , pp. 103-107
    • Scholz, G.1    Manteuffel, R.2    Müntz, K.3    Rudolph, A.4
  • 98
    • 0026556773 scopus 로고
    • A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean
    • Scott MP, Jung R, Müntz K, Nielsen NC. 1992. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proceedings of the National Academy of Sciences USA 89, 658-62.
    • (1992) Proceedings of the National Academy of Sciences USA , vol.89 , pp. 658-662
    • Scott, M.P.1    Jung, R.2    Müntz, K.3    Nielsen, N.C.4
  • 99
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • Shewry PR, Tatham AS. 1990. The prolamin storage proteins of cereal seeds: structure and evolution. Biochemical Journal 267, 1-12.
    • (1990) Biochemical Journal , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 100
    • 0028446555 scopus 로고
    • Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms
    • Shimada T, Hiraiwa N, Nishimura M, Hara-Nishimura I. 1994. Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms. Plant Cell Physiology 35, 713-18.
    • (1994) Plant Cell Physiology , vol.35 , pp. 713-718
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 101
    • 5844324796 scopus 로고
    • Primary changes of reserve proteins during germination of vetch seeds
    • In Russian
    • Shutov AD, Vaintraub IA. 1973. Primary changes of reserve proteins during germination of vetch seeds Fiziologia Rastenji 20, 504-9 (In Russian).
    • (1973) Fiziologia Rastenji , vol.20 , pp. 504-509
    • Shutov, A.D.1    Vaintraub, I.A.2
  • 102
    • 0000024298 scopus 로고
    • Degradation of storage proteins in germinating seeds
    • Shutov A, Vaintraub IA. 1987. Degradation of storage proteins in germinating seeds. Phytochemistry 26, 1557-66.
    • (1987) Phytochemistry , vol.26 , pp. 1557-1566
    • Shutov, A.1    Vaintraub, I.A.2
  • 104
    • 0039372307 scopus 로고
    • High molecular weight products of hydrolysis of soybean glycinin by trypsin
    • Shutov AD, Senyuk VI, Kakhovskaya IA, Pineda J. 1993. High molecular weight products of hydrolysis of soybean glycinin by trypsin. Biokhimiya 58, 301-12.
    • (1993) Biokhimiya , vol.58 , pp. 301-312
    • Shutov, A.D.1    Senyuk, V.I.2    Kakhovskaya, I.A.3    Pineda, J.4
  • 105
    • 0022432415 scopus 로고
    • Nucleotide sequences from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris are encoded by two unique gene families
    • Slightom JL, Drong RF, Klassy RC, Hoffman LM. 1985. Nucleotide sequences from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Research 18, 6483-98.
    • (1985) Nucleic Acids Research , vol.18 , pp. 6483-6498
    • Slightom, J.L.1    Drong, R.F.2    Klassy, R.C.3    Hoffman, L.M.4
  • 106
    • 0002635994 scopus 로고
    • Novel regulation of vegetative storage protein genes
    • Staswick PE. 1990. Novel regulation of vegetative storage protein genes. The Plant Cell 2, 1-6.
    • (1990) The Plant Cell , vol.2 , pp. 1-6
    • Staswick, P.E.1
  • 109
    • 0010242584 scopus 로고
    • Expression of an endopeptidase (EP-C1) in Phaseolus vulgaris plants
    • Tanaka T, Minamikawa T, Yamauchi D, Ogushi Y. 1993 Expression of an endopeptidase (EP-C1) in Phaseolus vulgaris plants. Plant Physiology 101, 421-8.
    • (1993) Plant Physiology , vol.101 , pp. 421-428
    • Tanaka, T.1    Minamikawa, T.2    Yamauchi, D.3    Ogushi, Y.4
  • 110
    • 0026176684 scopus 로고
    • Nucleotide sequence for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits
    • Tanaka T, Yamauchi D, Minamikawa T. 1991. Nucleotide sequence for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits. Plant Molecular Biology 16, 1083-4.
    • (1991) Plant Molecular Biology , vol.16 , pp. 1083-1084
    • Tanaka, T.1    Yamauchi, D.2    Minamikawa, T.3
  • 111
    • 0017598953 scopus 로고
    • Beta-conglycinin from soybean proteins. Isolation and immunological and physico-chemical properties of the monomeric forms
    • Thanh VH, Shibasaki K. 1977. Beta-conglycinin from soybean proteins. Isolation and immunological and physico-chemical properties of the monomeric forms. Biochimica et Biophysica Acta 490, 370-84.
    • (1977) Biochimica et Biophysica Acta , vol.490 , pp. 370-384
    • Thanh, V.H.1    Shibasaki, K.2
  • 112
    • 0026568549 scopus 로고
    • Protein deamidase from germinating wheat grains
    • Vaintraub IA, Kotova LV, Shaha R. 1992. Protein deamidase from germinating wheat grains. FEBS Letters 302, 169-71.
    • (1992) FEBS Letters , vol.302 , pp. 169-171
    • Vaintraub, I.A.1    Kotova, L.V.2    Shaha, R.3
  • 114
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Vitale A, Ceriotti A, Denecke J. 1993. The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. Journal of Experimental Botany 44, 1417-44.
    • (1993) Journal of Experimental Botany , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 115
    • 0024301301 scopus 로고
    • In vitro mutated phytohemaglutinin genes expressed in tobacco seeds: Role of glycans in protein targeting and stability
    • Voelker TA, Herman EM, Chrispeels MJ. 1989. In vitro mutated phytohemaglutinin genes expressed in tobacco seeds: role of glycans in protein targeting and stability. The Plant Cell 1, 95-104.
    • (1989) The Plant Cell , vol.1 , pp. 95-104
    • Voelker, T.A.1    Herman, E.M.2    Chrispeels, M.J.3
  • 117
    • 0002150829 scopus 로고
    • Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed
    • Dalling MJ, ed. Boca Raton, Florida: CRC Press Inc.
    • Wilson KA. 1986. Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed. 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
  • 118
    • 0002581206 scopus 로고
    • Differential proteolysis of glycinin and β-conglycinin polypeptides during soybean germination and seedling growth
    • Wilson KA, Rightmire BR, Chen JC, Tan-Wilson AL. 1986. Differential proteolysis of glycinin and β-conglycinin polypeptides during soybean germination and seedling growth. Plant Physiology 82, 71-6.
    • (1986) Plant Physiology , vol.82 , pp. 71-76
    • Wilson, K.A.1    Rightmire, B.R.2    Chen, J.C.3    Tan-Wilson, A.L.4
  • 119
    • 0000220251 scopus 로고
    • Cysteine endopeptidase from Vigna mungo: Gene structure and expression
    • Yamauchi D, Akasofu H, Minamikawa T. 1992. Cysteine endopeptidase from Vigna mungo: gene structure and expression. Plant Cell Physiology 33, 789-97.
    • (1992) Plant Cell Physiology , vol.33 , pp. 789-797
    • Yamauchi, D.1    Akasofu, H.2    Minamikawa, T.3
  • 120
    • 0028092248 scopus 로고
    • Purification and characterization of a cysteine proteinase involved in globulin hydrolysation in germinated Vicia faba L.
    • Yu WJ, Greenwood JS. 1992. Purification and characterization of a cysteine proteinase involved in globulin hydrolysation in germinated Vicia faba L. Journal of Experimental Botany 45, 261-8.
    • (1992) Journal of Experimental Botany , vol.45 , pp. 261-268
    • Yu, W.J.1    Greenwood, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.