메뉴 건너뛰기




Volumn 275, Issue 21, 2008, Pages 5429-5443

Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus

Author keywords

Cathepsin B; Cotyledon; Cysteine protease; Germination; Occluding loop

Indexed keywords

2 DIETHYLAMINOETHANOL; AMIDE; ANTIPAIN; CATHEPSIN B; CELLULOSE; CHYMOSTATIN; COMPLEMENTARY DNA; CORTICOTROPIN; CYSTATIN; CYSTEINE PROTEINASE; DIPEPTIDYL CARBOXYPEPTIDASE; EGG WHITE; EXOPEPTIDASE; HYDROXYAPATITE; IODOACETAMIDE; LEUCINE; LEUPEPTIN; N (3 PROPYLCARBAMOYLOXIRANE 2 CARBONYL)ISOLEUCYLPROLINE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; ORGANOMERCURY COMPOUND; PEPTIDASE; PHENYLALANINE; SEPHAROSE; TOSYLLYSYL CHLOROMETHYL KETONE;

EID: 53849141182     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06674.x     Document Type: Article
Times cited : (14)

References (44)
  • 2
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: Regulatory function of plant proteases
    • Schaller A (2004) A cut above the rest: regulatory function of plant proteases. Planta 220, 183 197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 3
    • 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]. J Biochem 126, 296 301.
    • (1999) J Biochem , vol.126 , pp. 296-301
    • Asano, M.1    Suzuki, S.2    Kawai, M.3    Miwa, T.4    Shibai, H.5
  • 4
    • 0002898965 scopus 로고
    • Purification and characterization of gibberellic acid-induced cysteine endoproteases in barley aleurone layers
    • Koehler S Ho T-H D (1988) Purification and characterization of gibberellic acid-induced cysteine endoproteases in barley aleurone layers. Plant Physiol 87, 95 103.
    • (1988) Plant Physiol , vol.87 , pp. 95-103
    • Koehler, S.1    Ho -H, T.D.2
  • 5
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endopeptidase with a C-terminal KDEL motif isolated from caster bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment
    • Schmid M, Simpson D, Kalousek F Gietl C (1998) A cysteine endopeptidase with a C-terminal KDEL motif isolated from caster bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment. Planta 206, 466 475.
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, C.4
  • 6
    • 2542450034 scopus 로고    scopus 로고
    • Molecular cloning, functional expression in Escherichia coli and enzymatic characterization of a cysteine protease from white clover (Trifolium repens)
    • Asp T, Bowra S, Borg S Holm PB (2004) Molecular cloning, functional expression in Escherichia coli and enzymatic characterization of a cysteine protease from white clover (Trifolium repens). Biochem Biophys Acta 1699, 111 122.
    • (2004) Biochem Biophys Acta , vol.1699 , pp. 111-122
    • Asp, T.1    Bowra, S.2    Borg, S.3    Holm, P.B.4
  • 7
    • 0026953035 scopus 로고
    • A gibberellin-regulated gene from wheat with sequence homology to cathepsin B of mammalian cells
    • Cejudo FJ, Murphy G, Chinoy C Baulcombe DC (1992) A gibberellin-regulated gene from wheat with sequence homology to cathepsin B of mammalian cells. Plant J 2, 937 948.
    • (1992) Plant J , vol.2 , pp. 937-948
    • Cejudo, F.J.1    Murphy, G.2    Chinoy, C.3    Baulcombe, D.C.4
  • 8
    • 0842323769 scopus 로고    scopus 로고
    • Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistances to Phytophthora infestans
    • Avrova AO, Taleb N, Rokka V-M, Heilbronn J, Campbell E, Hein I, Gilroy EM, Cardle L, Bradshaw JE, Stewart HE et al. (2004) Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistances to Phytophthora infestans. Mol Plant Pathol 5, 45 56.
    • (2004) Mol Plant Pathol , vol.5 , pp. 45-56
    • Avrova, A.O.1    Taleb, N.2    Rokka, V.-M.3    Heilbronn, J.4    Campbell, E.5    Hein, I.6    Gilroy, E.M.7    Cardle, L.8    Bradshaw, J.E.9    Stewart, H.E.10
  • 9
    • 0029379667 scopus 로고
    • Isolation and expression pattern of a cDNA encoding a cathepsin B-like protease from Nicotiana rustica
    • Lidett AJ, Moran M, Wong KAL, Furze J, Rhodes MJC Hamill JD (1995) Isolation and expression pattern of a cDNA encoding a cathepsin B-like protease from Nicotiana rustica. Plant Mol Biol 29, 379 384.
    • (1995) Plant Mol Biol , vol.29 , pp. 379-384
    • Lidett, A.J.1    Moran, M.2    Wong, K.A.L.3    Furze, J.4    Rhodes, M.J.C.5    Hamill, J.D.6
  • 11
    • 0017886726 scopus 로고
    • The specificity of cathepsin B. Hydrolysis of glucagons at the C-terminus by a peptidyldipeptidase mechanism
    • Aronson NN Jr. Barrett AJ (1978) The specificity of cathepsin B. Hydrolysis of glucagons at the C-terminus by a peptidyldipeptidase mechanism. Biochem J 171, 759 765.
    • (1978) Biochem J , vol.171 , pp. 759-765
    • Aronson Jr., N.N.1    Barrett, A.J.2
  • 12
    • 0040084898 scopus 로고    scopus 로고
    • Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts
    • Nägler DK, Storer AC, Portano FCV, Camona E, Juliano L Ménard R (1997) Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts. Biochemistry 36, 12608 12615.
    • (1997) Biochemistry , vol.36 , pp. 12608-12615
    • Nägler, D.K.1    Storer, A.C.2    Portano, F.C.V.3    Camona, E.4    Juliano, L.5    Ménard, R.6
  • 15
  • 16
    • 0028908350 scopus 로고
    • Crystal structure of cathepsin B inhibited with CA030 at 2.0-Å resolution: A basis for the design of specific epoxysuccinyl inhibitors
    • Turk D, Podobnik M, Popovic T, Katunuma N, Bode W, Huber R Turk V (1995) Crystal structure of cathepsin B inhibited with CA030 at 2.0-Å resolution: a basis for the design of specific epoxysuccinyl inhibitors. Biochemistry 34, 4791 4797.
    • (1995) Biochemistry , vol.34 , pp. 4791-4797
    • Turk, D.1    Podobnik, M.2    Popovic, T.3    Katunuma, N.4    Bode, W.5    Huber, R.6    Turk, V.7
  • 18
    • 0000249898 scopus 로고
    • Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs
    • Chan SJ, San Segundo B, McCormick MB Steiner DF (1986) Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc Natl Acad Sci USA 83, 7721 7725.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7721-7725
    • Chan, S.J.1    San Segundo, B.2    McCormick, M.B.3    Steiner, D.F.4
  • 19
    • 0027295815 scopus 로고
    • Nucleotide sequence of bovine preprocathepsin B. a study of polymorphism in the protein coding region
    • Mordier S, Bechet D, Roux MP, Obled A Ferrara M (1993) Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region. Biochim Biophys Acta 1174, 305 311.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 305-311
    • Mordier, S.1    Bechet, D.2    Roux, M.P.3    Obled, A.4    Ferrara, M.5
  • 20
    • 0029128688 scopus 로고
    • Avian cathepsin B cDNA: Sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme
    • Dong SS, Stransky GI, Whitaker CH, Jordan SE, Schlesinger PH, Edwards JC Blair HC (1995) Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme. Biochim Biophys Acta 1251, 69 73.
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 69-73
    • Dong, S.S.1    Stransky, G.I.2    Whitaker, C.H.3    Jordan, S.E.4    Schlesinger, P.H.5    Edwards, J.C.6    Blair, H.C.7
  • 21
    • 34447644452 scopus 로고    scopus 로고
    • Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L
    • Prabhakar S, Chen MS, Elpidina EN, Vinokurov KS, Smith CM, Marshall J Oppert B (2007) Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L. Insect Mol Biol 16, 455 468.
    • (2007) Insect Mol Biol , vol.16 , pp. 455-468
    • Prabhakar, S.1    Chen, M.S.2    Elpidina, E.N.3    Vinokurov, K.S.4    Smith, C.M.5    Marshall, J.6    Oppert, B.7
  • 22
    • 0032811124 scopus 로고    scopus 로고
    • Defined characteristics of cathepsin B-like proteins from nematodes: Inferred functional diversity and phylogenetic relationship
    • Rehman A Jasmer DP (1999) Defined characteristics of cathepsin B-like proteins from nematodes: inferred functional diversity and phylogenetic relationship. Mol Biochem Parasitol 102, 297 310.
    • (1999) Mol Biochem Parasitol , vol.102 , pp. 297-310
    • Rehman, A.1    Jasmer, D.P.2
  • 23
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid M McKerrow JH (2002) Cysteine proteases of parasitic organisms. Mol Biol Parasitol 120, 1 21.
    • (2002) Mol Biol Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 24
    • 38649117560 scopus 로고    scopus 로고
    • Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate Monocercomonides
    • Dacks JB, Kuru T, Liapounova NA Gedamu L (2008) Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate Monocercomonides. J Eukaryot Microbiol 55, 9 17.
    • (2008) J Eukaryot Microbiol , vol.55 , pp. 9-17
    • Dacks, J.B.1    Kuru, T.2    Liapounova, N.A.3    Gedamu, L.4
  • 26
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nägler DK, Zhang R, Tam W, Sulea T, Purisima EO Ménard R (1999) Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry 38, 12648 12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nägler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Ménard, R.6
  • 29
    • 0242599721 scopus 로고    scopus 로고
    • Crystal structure of cathepsin X: A flip-flop of the ring of H23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
    • Gunčar G, Klemenčič I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L Turk D (2000) Crystal structure of cathepsin X: a flip-flop of the ring of H23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. Structure 8, 305 313.
    • (2000) Structure , vol.8 , pp. 305-313
    • Gunčar, G.1    Klemenčič, I.2    Turk, B.3    Turk, V.4    Karaoglanovic-Carmona, A.5    Juliano, L.6    Turk, D.7
  • 30
    • 0034723144 scopus 로고    scopus 로고
    • Crystal structure of human procathepsin X: A cysteine protease with the proregion covalently linked to the active site cysteine
    • Sivaraman J, Nägler DK, Zhang R, Ménard R Cygler M (2000) Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. J Mol Biol 295, 939 951.
    • (2000) J Mol Biol , vol.295 , pp. 939-951
    • Sivaraman, J.1    Nägler, D.K.2    Zhang, R.3    Ménard, R.4    Cygler, M.5
  • 32
    • 0030961306 scopus 로고    scopus 로고
    • Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex
    • Yamamoto A, Hara T, Tomoo K, Ishida T, Fujii T, Hata Y, Murata M Kitamura K (1997) Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex. J Biochem 121, 974 977.
    • (1997) J Biochem , vol.121 , pp. 974-977
    • Yamamoto, A.1    Hara, T.2    Tomoo, K.3    Ishida, T.4    Fujii, T.5    Hata, Y.6    Murata, M.7    Kitamura, K.8
  • 33
    • 0024494090 scopus 로고
    • Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene. Expression in E. coli as fusion protein and its isolation
    • Auerswald E, Genenger G, Assfalg-Machleidt I, Kos J Bode W (1989) Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene. Expression in E. coli as fusion protein and its isolation. FEBS Lett 243, 186 192.
    • (1989) FEBS Lett , vol.243 , pp. 186-192
    • Auerswald, E.1    Genenger, G.2    Assfalg-Machleidt, I.3    Kos, J.4    Bode, W.5
  • 34
    • 0035865223 scopus 로고    scopus 로고
    • A cystatin-based affinity procedure for the isolation and analysis of papain-like cysteine proteinases from tissue extracts
    • Tombaccini D, Mocali A, Weber E Paoletti F (2001) A cystatin-based affinity procedure for the isolation and analysis of papain-like cysteine proteinases from tissue extracts. Anal Biochem 289, 231 238.
    • (2001) Anal Biochem , vol.289 , pp. 231-238
    • Tombaccini, D.1    Mocali, A.2    Weber, E.3    Paoletti, F.4
  • 35
    • 33750988212 scopus 로고    scopus 로고
    • The proteolytic processing of seed storage proteins in Arabidopsis embryo cells starts in the multivesicular bodies
    • Otegui M, Herder R, Schulze J, Jung R Staehelin LA (2006) The proteolytic processing of seed storage proteins in Arabidopsis embryo cells starts in the multivesicular bodies. Plant Cell 18, 2567 2581.
    • (2006) Plant Cell , vol.18 , pp. 2567-2581
    • Otegui, M.1    Herder, R.2    Schulze, J.3    Jung, R.4    Staehelin, L.A.5
  • 36
    • 34247195473 scopus 로고    scopus 로고
    • Protein storage vacuole acidification as a control of storage protein mobilization in soybeans
    • He F, Huang F, Wilson KA Tan-Wilson A (2007) Protein storage vacuole acidification as a control of storage protein mobilization in soybeans. J Exp Bot 58, 1059 1070.
    • (2007) J Exp Bot , vol.58 , pp. 1059-1070
    • He, F.1    Huang, F.2    Wilson, K.A.3    Tan-Wilson, A.4
  • 37
    • 0015606478 scopus 로고
    • Human cathepsin B1. Purification and some properties of the enzyme
    • Barrett A (1973) Human cathepsin B1. Purification and some properties of the enzyme. Biochem J 131, 809 822.
    • (1973) Biochem J , vol.131 , pp. 809-822
    • Barrett, A.1
  • 39
    • 0024455444 scopus 로고
    • Isolation and characterization of a novel large protease accumulated in mammalian cells in the presence of inhibitors
    • Tsuji A Kurachi K (1989) Isolation and characterization of a novel large protease accumulated in mammalian cells in the presence of inhibitors. J Biol Chem 264, 16093 16099.
    • (1989) J Biol Chem , vol.264 , pp. 16093-16099
    • Tsuji, A.1    Kurachi, K.2
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis BJ (1964) Disc electrophoresis. II. Method and application to human serum proteins. Ann NY Acad Sci 121, 404 427.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bateriophage T4
    • Laemmli UK (1970) Cleavage of structure proteins during the assembly of the head of bateriophage T4. Natute 227, 680 685.
    • (1970) Natute , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 14944345900 scopus 로고    scopus 로고
    • Identification of oligopeptidase B in higher plants. Purification and characterization of oligopeptidase B from quiescent wheat embryo, Triticum aestivum
    • Tsuji A, Yuasa K Matsuda Y (2004) Identification of oligopeptidase B in higher plants. Purification and characterization of oligopeptidase B from quiescent wheat embryo, Triticum aestivum. J Biochem 136, 673 681.
    • (2004) J Biochem , vol.136 , pp. 673-681
    • Tsuji, A.1    Yuasa, K.2    Matsuda, Y.3
  • 44
    • 0020473244 scopus 로고
    • Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier
    • Tian W-X Tsou C-L (1982) Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 21, 1028 1032.
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.-X.1    Tsou, C.-L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.