메뉴 건너뛰기




Volumn 263, Issue 3, 1999, Pages 726-735

Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato

Author keywords

Aminopeptidases; Defense response; Exopeptidases; Proteolysis; Wounding

Indexed keywords

AMASTATIN; BESTATIN; CYTOSOL AMINOPEPTIDASE; PROTEIN PRECURSOR;

EID: 0033179180     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00548.x     Document Type: Article
Times cited : (69)

References (61)
  • 1
    • 0014962699 scopus 로고
    • Purification and properties of an aminopeptidase from Escherichia coli
    • 1. Vogt, V. (1970) Purification and properties of an aminopeptidase from Escherichia coli. J. Biol. Chem. 245, 4760-4769.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4760-4769
    • Vogt, V.1
  • 2
    • 0024316734 scopus 로고
    • XerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase
    • 2. Stirling, C.J., Colloms, S.D., Collins, J.F., Szatmari, G. & Sherratt, D.J. (1989) xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J. 8, 1623-1627.
    • (1989) EMBO J. , vol.8 , pp. 1623-1627
    • Stirling, C.J.1    Colloms, S.D.2    Collins, J.F.3    Szatmari, G.4    Sherratt, D.J.5
  • 3
    • 0028237249 scopus 로고
    • Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination
    • 3. McCulloch, R., Burke, M.E. & Sherratt, D.J. (1994) Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol. 12, 241-251.
    • (1994) Mol. Microbiol. , vol.12 , pp. 241-251
    • McCulloch, R.1    Burke, M.E.2    Sherratt, D.J.3
  • 4
    • 0020360510 scopus 로고
    • Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lens and ability of bovine lens LAP to cleave bovine crystallins
    • 4. Taylor, A., Daims, M., Lee, J. & Surgenor, T. (1982) Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lens and ability of bovine lens LAP to cleave bovine crystallins. Eye Res. 2, 47-56.
    • (1982) Eye Res. , vol.2 , pp. 47-56
    • Taylor, A.1    Daims, M.2    Lee, J.3    Surgenor, T.4
  • 5
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • 5. Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Sci. USA 93, 12142-12149.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 6
    • 0009648652 scopus 로고    scopus 로고
    • Methionine aminopeptidase: Structure and function
    • (Taylor, A., ed.). RG Landes Co., Austin, Texas
    • 6. Bradshaw, R.A. & Arfin, S.M. (1996) Methionine aminopeptidase: structure and function. In Aminopeptidases (Taylor, A., ed.), pp. 91-112. RG Landes Co., Austin, Texas.
    • (1996) Aminopeptidases , pp. 91-112
    • Bradshaw, R.A.1    Arfin, S.M.2
  • 7
    • 0026649381 scopus 로고
    • Induction of leucine aminopeptidase by interferon-γ. Identification by protein microsequencing after purification by preparative two-dimensional gel electrophoresis
    • 7. Harris, C.A., Hunter, B., Krauses, M.R., Taylor, A. & Epstein, L.B. (1992) Induction of leucine aminopeptidase by interferon-γ. Identification by protein microsequencing after purification by preparative two-dimensional gel electrophoresis. J. Biol. Chem. 267, 6865-6869.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6865-6869
    • Harris, C.A.1    Hunter, B.2    Krauses, M.R.3    Taylor, A.4    Epstein, L.B.5
  • 8
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • 8. Beninga, J., Rock, K.L. & Goldberg, A.L. (1998) Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273, 18734-18742.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 9
    • 0015918807 scopus 로고
    • 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content
    • 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content. J. Biol. Chem. 248, 294-304.
    • (1973) J. Biol. Chem. , vol.248 , pp. 294-304
    • Carpenter, F.H.1    Vahl, J.M.2
  • 10
    • 0027237615 scopus 로고
    • Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin
    • 10. Kim, H., Burley, S.K. & Lipscomb, W.N. (1993) Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin. Biochemistry 32, 8465-8478.
    • (1993) Biochemistry , vol.32 , pp. 8465-8478
    • Kim, H.1    Burley, S.K.2    Lipscomb, W.N.3
  • 11
    • 0027237615 scopus 로고
    • X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: Formulation of a catalytic mechanism featuring a gem-diolate transition state
    • 11. Kim, H. & Lipscomb, W.N. (1993) X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state. Biochemistry 32, 8465-8478.
    • (1993) Biochemistry , vol.32 , pp. 8465-8478
    • Kim, H.1    Lipscomb, W.N.2
  • 12
    • 0029116127 scopus 로고
    • Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form
    • 12. Sträter, N. & Lipscomb, W.N. (1995) Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form. Biochemistry 34, 9200-9210.
    • (1995) Biochemistry , vol.34 , pp. 9200-9210
    • Sträter, N.1    Lipscomb, W.N.2
  • 13
    • 0028045722 scopus 로고
    • Structure and mechanism of bovine lens leucine aminopeptidase
    • 13. Kim, H. & Lipscomb, W.N. (1994) Structure and mechanism of bovine lens leucine aminopeptidase. Adv. Enzymol. Rel. Areas Mol. Biol. 68, 153-213.
    • (1994) Adv. Enzymol. Rel. Areas Mol. Biol. , vol.68 , pp. 153-213
    • Kim, H.1    Lipscomb, W.N.2
  • 14
    • 0003189112 scopus 로고    scopus 로고
    • Structure and function of bovine lens aminopeptidase and comparison with homologous aminopeptidases
    • (Taylor, A., ed.). RG Landes Co., Austin, Texas
    • 14. Taylor, A., Sanford, D. & Nowell, T. (1996) Structure and function of bovine lens aminopeptidase and comparison with homologous aminopeptidases. In Aminopeptidases (Taylor, A., ed.), pp. 21-67. RG Landes Co., Austin, Texas.
    • (1996) Aminopeptidases , pp. 21-67
    • Taylor, A.1    Sanford, D.2    Nowell, T.3
  • 15
    • 0026514586 scopus 로고
    • Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants
    • 15. Bartling, D. & Weiler, E.W. (1992) Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. Eur. J. Biochem. 205, 425-431.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 425-431
    • Bartling, D.1    Weiler, E.W.2
  • 16
    • 0026918137 scopus 로고
    • General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding
    • 16. Hildmann, T., Ebneth, M, Peña-Cortés, H., Sánchez-Serrano, J.J., Willmitzer, L. & Prat, S. (1992) General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 4, 1157-1170.
    • (1992) Plant Cell , vol.4 , pp. 1157-1170
    • Hildmann, T.1    Ebneth, M.2    Peña-Cortés, H.3    Sánchez-Serrano, J.J.4    Willmitzer, L.5    Prat, S.6
  • 17
    • 0027490705 scopus 로고
    • Leucine aminopeptidase: An inducible component of the defense response in Lycopersicon esculentum (tomato)
    • 17. Pautot, V., Holzer, F.M., Reisch, B. & Walling, L.L. (1993) Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato). Proc. Natl Acad. Sci. USA 90, 9906-9910.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9906-9910
    • Pautot, V.1    Holzer, F.M.2    Reisch, B.3    Walling, L.L.4
  • 18
    • 0029959103 scopus 로고    scopus 로고
    • Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato
    • 18. Gu, Y.-Q., Chao, W.S. & Walling, L.L. (1996) Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato. J. Biol. Chem. 271, 25880-25887.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25880-25887
    • Gu, Y.-Q.1    Chao, W.S.2    Walling, L.L.3
  • 19
    • 0000605950 scopus 로고    scopus 로고
    • Plant aminopeptidases: Occurrence, function and characterization
    • (Taylor, A., ed.). RG Landes Co, Austin, Texas
    • 19. Walling, L.L. & Gu, Y.-Q. (1996) Plant aminopeptidases: occurrence, function and characterization. In Aminopeptidases (Taylor, A., ed.), pp. 173-219. RG Landes Co, Austin, Texas.
    • (1996) Aminopeptidases , pp. 173-219
    • Walling, L.L.1    Gu, Y.-Q.2
  • 20
    • 0000601032 scopus 로고    scopus 로고
    • A complex array of proteins related to the multimeric leucine aminopeptidase of tomato
    • 20. Gu, Y.-Q., Pautot, V., Holzer, F.M. & Walling, L.L. (1996) A complex array of proteins related to the multimeric leucine aminopeptidase of tomato. Plant Physiol. 110, 1257-1266.
    • (1996) Plant Physiol. , vol.110 , pp. 1257-1266
    • Gu, Y.-Q.1    Pautot, V.2    Holzer, F.M.3    Walling, L.L.4
  • 21
    • 0028121331 scopus 로고
    • Molecular and immunological characterization of leucine aminopeptidase in Arabidopsis thaliana: A new antibody suggests a semi-constitutive regulation of a phylogenetically old enzyme
    • 21. Bartling, D. & Nosek, J. (1994) Molecular and immunological characterization of leucine aminopeptidase in Arabidopsis thaliana: a new antibody suggests a semi-constitutive regulation of a phylogenetically old enzyme. Plant. Sci. 9, 199-209.
    • (1994) Plant. Sci. , vol.9 , pp. 199-209
    • Bartling, D.1    Nosek, J.2
  • 22
    • 0032875708 scopus 로고    scopus 로고
    • Leucine aminopeptidase RNAs, proteins and activities increase in response to water deficit, salinity and the wound signals - Systemin, methyl jasmonate, and abscisic acid
    • in press
    • 22. Chao, W.S., Gu, Y.-Q., Pautot, V, Bray, E.A. & Walling, L.L. (1999) Leucine aminopeptidase RNAs, proteins and activities increase in response to water deficit, salinity and the wound signals - systemin, methyl jasmonate, and abscisic acid. Plant Physiol. in press.
    • (1999) Plant Physiol.
    • Chao, W.S.1    Gu, Y.-Q.2    Pautot, V.3    Bray, E.A.4    Walling, L.L.5
  • 23
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • 23. Varshavsky, A. (1997) The ubiquitin system. Trends Biochem. Sci. 22, 383-387.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 24
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • 24. Vierstra, R.D. (1996) Proteolysis in plants: mechanisms and functions. Plant Mol. Biol. 32, 275-302.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 25
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • 25. Callis, J. (1995) Regulation of protein degradation. Plant Cell 7, 845-857.
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • 27. Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 84988119829 scopus 로고
    • Quantitation of microgram amounts of protein in two-dimensional polyacrylamide gel electrophoresis sample buffer
    • 28. Ramagli, L.S. & Rodriguez, L.V. (1985) Quantitation of microgram amounts of protein in two-dimensional polyacrylamide gel electrophoresis sample buffer. Electrophoresis 6, 559-563.
    • (1985) Electrophoresis , vol.6 , pp. 559-563
    • Ramagli, L.S.1    Rodriguez, L.V.2
  • 29
    • 0026166366 scopus 로고
    • Expression of proteinase inhibitor genes during Pseudomonas syringe pv. tomato infection
    • 29. Pautot, V., Holzer, F.M. & Walling, L.L. (1991) Expression of proteinase inhibitor genes during Pseudomonas syringe pv. tomato infection. Molec. Plant-Microb. Inter. 4, 284-292.
    • (1991) Molec. Plant-Microb. Inter. , vol.4 , pp. 284-292
    • Pautot, V.1    Holzer, F.M.2    Walling, L.L.3
  • 30
    • 0001178697 scopus 로고
    • Patterns of protein accumulation in developing anthers of Lilium longiflorum correlate with histological events
    • 30. Wang, C.-S., Walling, L.L., Eckard, K.J. & Lord, E.M. (1992) Patterns of protein accumulation in developing anthers of Lilium longiflorum correlate with histological events. Plant Physiol. 99, 822-829.
    • (1992) Plant Physiol. , vol.99 , pp. 822-829
    • Wang, C.-S.1    Walling, L.L.2    Eckard, K.J.3    Lord, E.M.4
  • 31
    • 0017342164 scopus 로고
    • Molecular weights of protein multimers from polyacrylamide gel electrophoresis
    • 31. Bryan, J.K. (1977) Molecular weights of protein multimers from polyacrylamide gel electrophoresis. Anal Biochem. 78, 512-519.
    • (1977) Anal Biochem. , vol.78 , pp. 512-519
    • Bryan, J.K.1
  • 32
    • 0000052340 scopus 로고
    • Expression of low molecular weight heat-shock proteins under field conditions
    • 32. Hernandez, L.D. & Vierling, E. (1993) Expression of low molecular weight heat-shock proteins under field conditions. Plant Physiol. 101, 1209-1216.
    • (1993) Plant Physiol. , vol.101 , pp. 1209-1216
    • Hernandez, L.D.1    Vierling, E.2
  • 33
    • 0015103368 scopus 로고
    • Partial purification and enzymatic properties of an aminopeptidase from barley
    • 33. Kolehmainen, L. & Mikola, J. (1971) Partial purification and enzymatic properties of an aminopeptidase from barley. Arch. Biochem. Biophys. 145, 632-642.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 632-642
    • Kolehmainen, L.1    Mikola, J.2
  • 34
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • 34. Ellis, K.J. & Morrison, J.F. (1982) Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol. 87, 405-426.
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 35
    • 0018595598 scopus 로고
    • Limited tryptic digestion of bovine eye lens leucine aminopeptidase
    • 35. van Loon-Klaasen, L., Cuypers, H.T. & Bloemendal, H. (1979) Limited tryptic digestion of bovine eye lens leucine aminopeptidase. FEBS Lett. 107, 366-370.
    • (1979) FEBS Lett. , vol.107 , pp. 366-370
    • Van Loon-Klaasen, L.1    Cuypers, H.T.2    Bloemendal, H.3
  • 36
    • 0027380594 scopus 로고
    • Isolation of bovine kidney leucine aminopeptidase cDNA - Comparison with the lens enzyme and tissue specific expression of two messenger RNAs
    • 36. Wallner, B.P., Hession, C., Tizard, R., Frey, A.Z., Zuliani, A., Mura, C., Jahngen-Hodge, J. & Taylor, A. (1993) Isolation of bovine kidney leucine aminopeptidase cDNA - comparison with the lens enzyme and tissue specific expression of two messenger RNAs. Biochemistry 32, 9296-9301.
    • (1993) Biochemistry , vol.32 , pp. 9296-9301
    • Wallner, B.P.1    Hession, C.2    Tizard, R.3    Frey, A.Z.4    Zuliani, A.5    Mura, C.6    Jahngen-Hodge, J.7    Taylor, A.8
  • 37
    • 0019890799 scopus 로고
    • Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase
    • 37. van Wart, H.E. & Lin, S.H. (1981) Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase. Biochemistry 20, 5682-5689.
    • (1981) Biochemistry , vol.20 , pp. 5682-5689
    • Van Wart, H.E.1    Lin, S.H.2
  • 38
    • 0017741654 scopus 로고
    • Leucine aminopeptidase from swine kidney: Purification, molecular weight, subunit and amino acid composition
    • 38. Shen, C. & Melius, P. (1977) Leucine aminopeptidase from swine kidney: purification, molecular weight, subunit and amino acid composition. Prep Biochem. 7, 243-256.
    • (1977) Prep Biochem. , vol.7 , pp. 243-256
    • Shen, C.1    Melius, P.2
  • 39
    • 0015239427 scopus 로고
    • Leucine aminopeptidase (bovine lens)
    • 39. Melbye, S.W. & Carpenter, F.H. (1971) Leucine aminopeptidase (bovine lens). J. Biol. Chem. 246, 2459-2463.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2459-2463
    • Melbye, S.W.1    Carpenter, F.H.2
  • 40
    • 0001014396 scopus 로고
    • Purification and partial characterization of barley leucine aminopeptidase
    • 40. Sopanen, T. & Mikola, J. (1975) Purification and partial characterization of barley leucine aminopeptidase. Plant Physiol. 55, 809-814.
    • (1975) Plant Physiol. , vol.55 , pp. 809-814
    • Sopanen, T.1    Mikola, J.2
  • 41
    • 0019134669 scopus 로고
    • Comparative properties of genetically defined peptidases in maize
    • 41. Vodkin, L. & Scandalios, J. (1980) Comparative properties of genetically defined peptidases in maize. Biochemistry 19, 4660-4667.
    • (1980) Biochemistry , vol.19 , pp. 4660-4667
    • Vodkin, L.1    Scandalios, J.2
  • 42
    • 0000530521 scopus 로고
    • Partial purification and characterization of aminopeptidase II from Chara australis
    • 42. Moriyasu, Y. & Miyoshi, Y. (1989) Partial purification and characterization of aminopeptidase II from Chara australis. Plant Physiol. 89, 687-691.
    • (1989) Plant Physiol. , vol.89 , pp. 687-691
    • Moriyasu, Y.1    Miyoshi, Y.2
  • 43
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaparones and protein folding in plants
    • 43. Boston, R.S., Viitanen, P.V. & Vierling, E. (1996) Molecular chaparones and protein folding in plants. Plant Molec. Biol. 32, 191-222.
    • (1996) Plant Molec. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 44
    • 0017849792 scopus 로고
    • Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes
    • 44. Aoyagi, T., Tobe, H., Kojima, F., Hamada, M., Takeuchi, T. & Umezawa, H. (1978) Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes. J. Antibiot. 31, 636-638.
    • (1978) J. Antibiot. , vol.31 , pp. 636-638
    • Aoyagi, T.1    Tobe, H.2    Kojima, F.3    Hamada, M.4    Takeuchi, T.5    Umezawa, H.6
  • 45
    • 0017236348 scopus 로고
    • Bestatin, an inhibitor of aminopeptidase B, produced by actinomyces
    • 45. Umezawa, H., Aoyagi, T., Suda, H., Hamada, M. & Takeuchi, T. (1976). Bestatin, an inhibitor of aminopeptidase B, produced by actinomyces. J. Antibiot. 29, 97-99.
    • (1976) J. Antibiot. , vol.29 , pp. 97-99
    • Umezawa, H.1    Aoyagi, T.2    Suda, H.3    Hamada, M.4    Takeuchi, T.5
  • 46
    • 0014101014 scopus 로고
    • Struktur-und Wirkungsidentität der leucinaminopeptidase aus schweinenieren und rinderaugelnlinsen unde verglieich mit der partikelaminopeptidase aus schweinenieren
    • 46. Hanson, H., Clässer, D., Ludewig, M., Mannsfeldt, H. & John, M. (1967) Struktur-und Wirkungsidentität der leucinaminopeptidase aus schweinenieren und rinderaugelnlinsen unde verglieich mit der partikelaminopeptidase aus schweinenieren. Hoppe-Seyler Z. Physiol. Chem. 348, 689-704.
    • (1967) Hoppe-Seyler Z. Physiol. Chem. , vol.348 , pp. 689-704
    • Hanson, H.1    Clässer, D.2    Ludewig, M.3    Mannsfeldt, H.4    John, M.5
  • 47
    • 4243433119 scopus 로고
    • Zur aktivität unde spezifität der leucinaminopeptidase in augenlinsen. Aimnosäure-und dipeptidanilide als substrate
    • 47. Frittkau, S., Gläßer, D. & Hanson, H. (1960) Zur aktivität unde spezifität der leucinaminopeptidase in augenlinsen. Aimnosäure-und dipeptidanilide als substrate. Hoppe-Seyler Z. Physiol. Chem. 322, 101-111.
    • (1960) Hoppe-Seyler Z. Physiol. Chem. , vol.322 , pp. 101-111
    • Frittkau, S.1    Gläßer, D.2    Hanson, H.3
  • 48
    • 0025700685 scopus 로고
    • Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase
    • 48. Turzynski, A. & Mentlein, R. (1990) Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase. Eur. J. Biochem. 190, 509-515.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 509-515
    • Turzynski, A.1    Mentlein, R.2
  • 49
    • 0028003198 scopus 로고
    • Functional analysis of leucine aminopeptidase from Solanum tuberosum L
    • 49. Herbers, K., Prat, S. & Willmitzer, L. (1994) Functional analysis of leucine aminopeptidase from Solanum tuberosum L. Planta 194, 230-240.
    • (1994) Planta , vol.194 , pp. 230-240
    • Herbers, K.1    Prat, S.2    Willmitzer, L.3
  • 50
    • 0032033079 scopus 로고    scopus 로고
    • A -308 deletion of the tomato LAP promoters is able to direct flower-specific and MeJA-induced expression in transgenic plants
    • 50. Ruíz-Rivero, O. & Prat, S. (1998) A -308 deletion of the tomato LAP promoters is able to direct flower-specific and MeJA-induced expression in transgenic plants. Plant Mol. Biol. 36, 639-648.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 639-648
    • Ruíz-Rivero, O.1    Prat, S.2
  • 51
    • 0021919107 scopus 로고
    • Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase
    • 51. Andersson, L., MacNeela, J. & Wolfenden, R. (1985) Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase. Biochemistry 24, 330-333.
    • (1985) Biochemistry , vol.24 , pp. 330-333
    • Andersson, L.1    MacNeela, J.2    Wolfenden, R.3
  • 53
    • 0001524441 scopus 로고
    • Nucleotide sequence of the genes for the alpha, beta and epsilon subunits of wheat chloroplast ATP synthase
    • 53. Howe, C.J., Fearnley, I.M., Walker, J.E., Dyer, T.A. & Gray, J.C. (1985) Nucleotide sequence of the genes for the alpha, beta and epsilon subunits of wheat chloroplast ATP synthase. Plant Mol. Biol. 4, 333-345.
    • (1985) Plant Mol. Biol. , vol.4 , pp. 333-345
    • Howe, C.J.1    Fearnley, I.M.2    Walker, J.E.3    Dyer, T.A.4    Gray, J.C.5
  • 54
    • 0021770424 scopus 로고
    • Purification and partial amino acid sequence of the chloroplast cytochrome b-559
    • 54. Widger, W.R., Cramer, W.A., Hermodsen, M., Meyer, D. & Gullifor, M. (1984) Purification and partial amino acid sequence of the chloroplast cytochrome b-559. J. Biol. Chem. 259, 3870-3876.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3870-3876
    • Widger, W.R.1    Cramer, W.A.2    Hermodsen, M.3    Meyer, D.4    Gullifor, M.5
  • 55
    • 0022589701 scopus 로고
    • Purification and partial sequence of the Mr 10,000 phosphoprotein from spinach thylakoids
    • 55. Farchaus, J. & Dilley, W. (1986) Purification and partial sequence of the Mr 10,000 phosphoprotein from spinach thylakoids. Arch. Biochem. Biophys. 244, 94-101.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 94-101
    • Farchaus, J.1    Dilley, W.2
  • 56
    • 0001195817 scopus 로고
    • Protective action of midgut catalase in lepidopteran larvea against oxidative plant defenses
    • 56. Felton, G.W. & Duffey, S.S. (1991) Protective action of midgut catalase in lepidopteran larvea against oxidative plant defenses. J. Chem. Ecol. 17, 1821-1836.
    • (1991) J. Chem. Ecol. , vol.17 , pp. 1821-1836
    • Felton, G.W.1    Duffey, S.S.2
  • 57
    • 0029347066 scopus 로고
    • Association of a 33-kilodalton cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth
    • 57. Jiang, B., Siregar, U., Willeford, K.O., Luthe, D.S. & Williams, W.P. (1995) Association of a 33-kilodalton cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth. Plant Physiol. 108, 1631-1640.
    • (1995) Plant Physiol. , vol.108 , pp. 1631-1640
    • Jiang, B.1    Siregar, U.2    Willeford, K.O.3    Luthe, D.S.4    Williams, W.P.5
  • 58
    • 84989719235 scopus 로고
    • Purification and characterization of leucine aminopeptidase from kidney bean cotyledons
    • 58. Mikkonen, A. (1992) Purification and characterization of leucine aminopeptidase from kidney bean cotyledons. Physiol. Plant. 84, 393-398.
    • (1992) Physiol. Plant. , vol.84 , pp. 393-398
    • Mikkonen, A.1
  • 59
    • 0027160549 scopus 로고
    • Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography
    • 59. Kim, H. & Lipscomb, W.N. (1993) Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography. Proc. Natl Acad. Sci. USA 90, 5006-5010.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5006-5010
    • Kim, H.1    Lipscomb, W.N.2
  • 60
    • 0015912124 scopus 로고
    • Bovine lens leucine aminopeptidase. Kinetic studies with activators and competitive inhibitors
    • 60. Lasch, J., Kudernatsch, W. & Hanson, H. (1973) Bovine lens leucine aminopeptidase. Kinetic studies with activators and competitive inhibitors. Eur. J. Biochem. 34, 53-57.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 53-57
    • Lasch, J.1    Kudernatsch, W.2    Hanson, H.3
  • 61
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpA and ClpC, functional homologs of E. coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • 61. Shanklin, J., DeWitt, N.D. & Flanagan, J.M. (1995) The stroma of higher plant plastids contain ClpA and ClpC, functional homologs of E. coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant Cell 7, 1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.