메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Biochemical aspects of a serine protease from Caesalpinia echinata Lam. (Brazilwood) seeds: A potential tool to access the mobilization of seed storage proteins

Author keywords

[No Author keywords available]

Indexed keywords

SEED STORAGE PROTEIN; SERINE PROTEINASE; TOSYLLYSYL CHLOROMETHYL KETONE;

EID: 84862330033     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/2012/562715     Document Type: Article
Times cited : (7)

References (38)
  • 1
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: The regulatory function of plant proteases
    • DOI 10.1007/s00425-004-1407-2
    • Schaller A., A cut above the rest: the regulatory function of plant proteases Planta 2004 220 2 183 197 (Pubitemid 40084177)
    • (2004) Planta , vol.220 , Issue.2 , pp. 183-197
    • Schaller, A.1
  • 2
    • 0021405057 scopus 로고
    • Trypsin-like protease from soybean seeds. purification and some properties
    • Nishikata M., Trypsin-like protease from soybean seeds. purification and some properties Journal of Biochemistry 1984 95 4 1169 1177
    • (1984) Journal of Biochemistry , vol.95 , Issue.4 , pp. 1169-1177
    • Nishikata, M.1
  • 3
    • 0034297227 scopus 로고    scopus 로고
    • Purification and characterization of a basic amino acid-specific peptidase from seeds of jack bean (Canavalia ensiformis)
    • Oshikawa K., Aoki K. -I., Yoshino Y., Terada S., Purification and characterization of a basic amino acid-specific peptidase from seeds of jack bean (Canavalia ensiformis) Bioscience, Biotechnology and Biochemistry 2000 64 10 2186 2192
    • (2000) Bioscience, Biotechnology and Biochemistry , vol.64 , Issue.10 , pp. 2186-2192
    • Oshikawa, K.1    Aoki, K.-I.2    Yoshino, Y.3    Terada, S.4
  • 4
    • 33847665220 scopus 로고    scopus 로고
    • A comparative study of the expression of serine proteinases in quiescent seeds and in developing Canavalia ensiformis plants
    • DOI 10.1093/jxb/erl223
    • Demartini D. R., Wlodawer A., Carlini C. R., A comparative study of the expression of serine proteinases in quiescent seeds and in developing Canavalia ensiformis plants Journal of Experimental Botany 2007 58 3 521 532 (Pubitemid 46363196)
    • (2007) Journal of Experimental Botany , vol.58 , Issue.3 , pp. 521-532
    • Demartini, D.R.1    Wlodawer, A.2    Carlini, C.R.3
  • 5
    • 0001098671 scopus 로고
    • Characterization of the major protease involved in the soybean -conglycinin storage protein mobilization
    • Qi X., Wilson K. A., Tan-Wilson A. L., Characterization of the major protease involved in the soybean -conglycinin storage protein mobilization Plant Physiology 1992 99 2 725 733
    • (1992) Plant Physiology , vol.99 , Issue.2 , pp. 725-733
    • Qi, X.1    Wilson, K.A.2    Tan-Wilson, A.L.3
  • 6
    • 0002954416 scopus 로고
    • Characterization of the proteinase that initiates the degradation of the trypsin inhibitor in germinating mung beans (Vigna radiata)
    • Wilson K. A., Tan-Wilson A. L., Characterization of the proteinase that initiates the degradation of the trypsin inhibitor in germinating mung beans (Vigna radiata) Plant Physiology 1987 84 93 98
    • (1987) Plant Physiology , vol.84 , pp. 93-98
    • Wilson, K.A.1    Tan-Wilson, A.L.2
  • 8
    • 84878761164 scopus 로고    scopus 로고
    • Caesalpinia echinata. In: IUCN 2011. IUCN Red List of Threatened Species. Version 2011.1, 2011
    • Varty N.,. Caesalpinia echinata. In: IUCN 2011. IUCN Red List of Threatened Species. Version 2011.1, 2011, http://www.iucnredlist.org/
  • 11
    • 0000041312 scopus 로고
    • Initiation of the degradation of the Soybean Kunitz and Bowman-Birk trypsin inhibitors by a cysteine protease
    • Papastortsis G., Wilson K. A., Initiation of the degradation of the Soybean Kunitz and Bowman-Birk trypsin inhibitors by a cysteine protease Plant Physiology 1991 96 4 1086 1092 (Pubitemid 21914130)
    • (1991) Plant Physiology , vol.96 , Issue.4 , pp. 1086-1092
    • Papastortsis, G.1    Wilson, K.A.2
  • 12
    • 0028092355 scopus 로고
    • Development of endopeptidase activities in maize (Zea mays L.) endosperms
    • Mitsuhashi W., Oaks A., Development of endopeptidase activities in maize (Zea mays L.) endosperms Plant Physiology 1994 104 2 401 407
    • (1994) Plant Physiology , vol.104 , Issue.2 , pp. 401-407
    • Mitsuhashi, W.1    Oaks, A.2
  • 13
    • 11944259049 scopus 로고
    • Appearance of endoproteolytic enzymes during the germination of Barley
    • Wrobel R., Jones B. L., Appearance of endoproteolytic enzymes during the germination of Barley Plant Physiology 1992 100 3 1508 1516
    • (1992) Plant Physiology , vol.100 , Issue.3 , pp. 1508-1516
    • Wrobel, R.1    Jones, B.L.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Analytical Biochemistry 1976 72 1-2 248 254
    • (1976) Analytical Biochemistry , vol.72 , Issue.12 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970 227 5259 680 685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger B. F., Kokowsky N., Cohen W., The preparation and properties of two new chromogenic substrates of trypsin Archives of Biochemistry and Biophysics 1961 95 2 271 278
    • (1961) Archives of Biochemistry and Biophysics , vol.95 , Issue.2 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 17
    • 0028800908 scopus 로고
    • Serine and cysteine proteinase inhibitors prevent nitric oxide production by activated macrophages by interfering with transcription of the inducible NO synthase gene
    • Griscavage J. M., Wilk S., Ignarro L. J., Serine and cysteine proteinase inhibitors prevent nitric oxide production by activated macrophages by interfering with transcription of the inducible NO synthase gene Biochemical and Biophysical Research Communications 1995 215 2 721 729
    • (1995) Biochemical and Biophysical Research Communications , vol.215 , Issue.2 , pp. 721-729
    • Griscavage, J.M.1    Wilk, S.2    Ignarro, L.J.3
  • 18
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins, B, H and L
    • Barrett A. J., Kembhavi A. A., Brown M. A., L-trans-Epoxysuccinyl- leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins, B, H and L Biochemical Journal 1982 201 1 189 198 (Pubitemid 12038477)
    • (1982) Biochemical Journal , vol.201 , Issue.1 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3
  • 19
    • 0018194680 scopus 로고
    • Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides
    • Lively M. O., Powers J. C., Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides Biochimica et Biophysica Acta 1978 525 1 171 179 (Pubitemid 8370742)
    • (1978) Biochimica et Biophysica Acta , vol.525 , Issue.1 , pp. 171-179
    • Lively, M.O.1    Powers, J.C.2
  • 20
    • 0014404233 scopus 로고
    • Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine
    • Markwardt F., Landmann H., Walsmann P., Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine European Journal of Biochemistry 1968 6 4 502 506
    • (1968) European Journal of Biochemistry , vol.6 , Issue.4 , pp. 502-506
    • Markwardt, F.1    Landmann, H.2    Walsmann, P.3
  • 21
    • 0017272560 scopus 로고
    • Structures and activities of protease inhibitors of microbial origin
    • Umezawa H., Structures and activities of protease inhibitors of microbial origin Methods in Enzymology 1976 45 C 678 695
    • (1976) Methods in Enzymology , vol.45 , Issue.C , pp. 678-695
    • Umezawa, H.1
  • 23
    • 0014249252 scopus 로고
    • Soybean inhibitorsI. Separation and some properties of three inhibitors from commercial crude soybean trypsin inhibitor
    • Frattali V., Steiner R. F., Soybean inhibitorsI. Separation and some properties of three inhibitors from commercial crude soybean trypsin inhibitor Biochemistry 1968 7 521 530
    • (1968) Biochemistry , vol.7 , pp. 521-530
    • Frattali, V.1    Steiner, R.F.2
  • 25
    • 0000316399 scopus 로고
    • Survey of the proteolytic activities degrading the Kunitz trypsin inhibitor and glycinin in germinating soybeans (Glycine max)
    • Wilson K. A., Papastoitsis G., Hartl P., Tan-Wilson A. L., Survey of the proteolytic activities degrading the Kunitz trypsin inhibitor and glycinin in germinating soybeans (Glycine max) Plant Physiology 1988 88 355 360
    • (1988) Plant Physiology , vol.88 , pp. 355-360
    • Wilson, K.A.1    Papastoitsis, G.2    Hartl, P.3    Tan-Wilson, A.L.4
  • 26
    • 24344495312 scopus 로고    scopus 로고
    • Plant serine proteases: Biochemical, physiological and molecular features
    • DOI 10.1016/j.plaphy.2005.05.001, PII S0981942805001270
    • Anto C. M., Malcata F. X., Plant serine proteases: biochemical, physiological and molecular features Plant Physiology and Biochemistry 2005 43 7 637 650 (Pubitemid 41253443)
    • (2005) Plant Physiology and Biochemistry , vol.43 , Issue.7 , pp. 637-650
    • Antao, C.M.1    Malcata, F.X.2
  • 27
    • 62549122479 scopus 로고    scopus 로고
    • Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen
    • Mohamed Ahmed I. A., Morishima I., Babiker E. E., Mori N., Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen Phytochemistry 2009 70 4 483 491
    • (2009) Phytochemistry , vol.70 , Issue.4 , pp. 483-491
    • Mohamed Ahmed, I.A.1    Morishima, I.2    Babiker, E.E.3    Mori, N.4
  • 28
    • 0035341706 scopus 로고    scopus 로고
    • A serine endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim
    • DOI 10.1016/S0031-9422(00)00511-2, PII S0031942200005112
    • Uchikoba T., Hosoyamada S., Onjyo M., Arima K., Yonezawa H., Kaneda M., A serine endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim Phytochemistry 2001 57 1 1 5 (Pubitemid 32331969)
    • (2001) Phytochemistry , vol.57 , Issue.1 , pp. 1-5
    • Uchikoba, T.1    Hosoyamada, S.2    Onjyo, M.3    Arima, K.4    Yonezawa, H.5    Kaneda, M.6
  • 29
    • 0028587825 scopus 로고
    • Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor
    • Yamagata H., Masuzawa T., Nagaoka Y., Ohnishi T., Iwasaki T., Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor Journal of Biological Chemistry 1994 269 52 32725 32731
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.52 , pp. 32725-32731
    • Yamagata, H.1    Masuzawa, T.2    Nagaoka, Y.3    Ohnishi, T.4    Iwasaki, T.5
  • 30
    • 0000020977 scopus 로고
    • Partial purification and characterization of two peptide hydrolases from pea seeds
    • Caldwell J. B., Sparrow L. G., Partial purification and characterization of two peptide hydrolases from pea seeds Plant Physiology 1976 57 795 798
    • (1976) Plant Physiology , vol.57 , pp. 795-798
    • Caldwell, J.B.1    Sparrow, L.G.2
  • 31
    • 0028520025 scopus 로고
    • A serine protease in soybean seeds that acts specifically on the native alpha subunit of beta-conglycinin
    • Morita S., Fukase M., Hoshino K., Fukuda Y., Yamaguchi M., Morita Y., A serine protease in soybean seeds that acts specifically on the native alpha subunit of beta-conglycinin Plant and Cell Physiology 1994 35 7 1049 1056
    • (1994) Plant and Cell Physiology , vol.35 , Issue.7 , pp. 1049-1056
    • Morita, S.1    Fukase, M.2    Hoshino, K.3    Fukuda, Y.4    Yamaguchi, M.5    Morita, Y.6
  • 32
    • 0000250332 scopus 로고
    • Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin
    • Yamagata H., Ueno S, Iwasaki T., Isolation and characterization of a possible native cucumisin from developing melon fruits and its limited autolysis to cucumisin Agricultural and Biological Chemistry 1989 53 1009 1017
    • (1989) Agricultural and Biological Chemistry , vol.53 , pp. 1009-1017
    • Yamagata, H.1    Ueno, S.2    Iwasaki, T.3
  • 33
    • 0000715943 scopus 로고
    • Proteases from the sarcocarp of yellow snake-gourd
    • Uchikoba T., Horita H., Kaneda M., Proteases from the sarcocarp of yellow snake-gourd Phytochemistry 1990 29 6 1879 1881
    • (1990) Phytochemistry , vol.29 , Issue.6 , pp. 1879-1881
    • Uchikoba, T.1    Horita, H.2    Kaneda, M.3
  • 34
    • 0036939344 scopus 로고    scopus 로고
    • SEP-1 - A subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgate L. cv. Morex
    • DOI 10.1007/s00425-002-0823-4
    • Fontanini D., Jones B. L., SEP-1a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgate L. cv. Morex Planta 2002 215 6 885 893 (Pubitemid 36080246)
    • (2002) Planta , vol.215 , Issue.6 , pp. 885-893
    • Fontanini, D.1    Jones, B.L.2
  • 35
    • 27944487490 scopus 로고    scopus 로고
    • Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids
    • DOI 10.1016/j.molcatb.2005.08.007, PII S138111770500130X
    • Zhao H., Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids Journal of Molecular Catalysis B 2005 37 16 16 25 (Pubitemid 41674643)
    • (2005) Journal of Molecular Catalysis B: Enzymatic , vol.37 , Issue.1-6 , pp. 16-25
    • Zhao, H.1
  • 36
    • 49649158205 scopus 로고
    • On the complex formation between basic pancreatic trypsin inhibitor and TLCK-, TPCK-derivatives of -trypsin
    • Imhoff J. M., Keil-Dlouha V., On the complex formation between basic pancreatic trypsin inhibitor and TLCK-, TPCK-derivatives of -trypsin FEBS Letters 1971 12 6 345 348
    • (1971) FEBS Letters , vol.12 , Issue.6 , pp. 345-348
    • Imhoff, J.M.1    Keil-Dlouha, V.2
  • 38
    • 0025678423 scopus 로고
    • Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds
    • Belozersky M. A., Dunaevsky Y. E., Voskoboynikova N. E., Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds Biochemical Journal 1990 272 3 677 682
    • (1990) Biochemical Journal , vol.272 , Issue.3 , pp. 677-682
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Voskoboynikova, N.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.