메뉴 건너뛰기




Volumn 32, Issue 6, 2011, Pages 1151-1158

An antifungal peptide from Fagopyrum tataricum seeds

Author keywords

Fagopyrum tartaricum; Phytopathogenic fungi; Purification; Trypsin inhibitor

Indexed keywords

AMINO ACID; AMMONIUM SULFATE; ANTIFUNGAL AGENT; FAGOPYRUM TATARICUM EXTRACT; POLYPEPTIDE; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 79958014329     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2011.03.015     Document Type: Article
Times cited : (24)

References (45)
  • 2
    • 0028979542 scopus 로고
    • Complete amino acid sequence of the protease inhibitor from buckwheat seeds
    • M.A. Belozersky, Y.E. Dunaevsky, A.K. Musolyamov, and T.A. Egorov Complete amino acid sequence of the protease inhibitor from buckwheat seeds FEBS Lett 371 1995 264 266
    • (1995) FEBS Lett , vol.371 , pp. 264-266
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Musolyamov, A.K.3    Egorov, T.A.4
  • 4
    • 1842675786 scopus 로고    scopus 로고
    • Inhibitor families of plant origin: Classification and characterization
    • Springer Verlag Berlin
    • Y. Birk Inhibitor families of plant origin: classification and characterization Plant protease inhibitors 2003 Springer Verlag Berlin
    • (2003) Plant Protease Inhibitors
    • Birk, Y.1
  • 6
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • W. Bode, and R. Huber Natural protein proteinase inhibitors and their interaction with proteinases Eur J Biochem 204 1992 433 451
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities for proteins utilizing the principle of proteindye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of micrograms quantities for proteins utilizing the principle of proteindye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • A.M. Crestfield, S. Moore, and W.H. Stein The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins J Biol Chem 238 1963 622 627
    • (1963) J Biol Chem , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 10
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • M. Dixon The determination of enzyme inhibitor constants J Biochem 55 1953 170 171
    • (1953) J Biochem , vol.55 , pp. 170-171
    • Dixon, M.1
  • 11
    • 0028893996 scopus 로고
    • Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products
    • C. Domoney, T. Welham, C. Sidebottom, and J.L. Firmin Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products FEBS Lett 360 1995 15 20
    • (1995) FEBS Lett , vol.360 , pp. 15-20
    • Domoney, C.1    Welham, T.2    Sidebottom, C.3    Firmin, J.L.4
  • 13
    • 77956988073 scopus 로고    scopus 로고
    • Coexpression of potato type i and II proteinase inhibitors gives cotton plants protection against insect damage in the field
    • K.M. Dunse, J.A. Stevens, F.T. Lay, Y.M. Gaspar, R.L. Heath, and M.A. Anderson Coexpression of potato type I and II proteinase inhibitors gives cotton plants protection against insect damage in the field Proc Natl Acad Sci USA 107 2010 15011 15015
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15011-15015
    • Dunse, K.M.1    Stevens, J.A.2    Lay, F.T.3    Gaspar, Y.M.4    Heath, R.L.5    Anderson, M.A.6
  • 14
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteine residues in proteins as S-beta-(4-pyridylethyl) cysteine
    • M. Friedman, L.H. Krull, and J.F. Cavins The chromatographic determination of cystine and cysteine residues in proteins as S-beta-(4-pyridylethyl) cysteine J Biol Chem 245 1970 3868 3871
    • (1970) J Biol Chem , vol.245 , pp. 3868-3871
    • Friedman, M.1    Krull, L.H.2    Cavins, J.F.3
  • 16
    • 0033016160 scopus 로고    scopus 로고
    • Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo
    • DOI 10.1016/S0022-1910(98)00161-9, PII S0022191098001619
    • A.M.R. Gatehouse, E. Norton, G.M. Davison, S.M. Babbe, C.A. Newell, and J.A. Gatehouse Digestive proteolytic activity in larvae of tomato moth Lacanobia oleracea effects of plant proteinase inhibitor in vitro and in vivo J Insect Physiol 45 1999 545 558 (Pubitemid 29242070)
    • (1999) Journal of Insect Physiology , vol.45 , Issue.6 , pp. 545-558
    • Gatehouse, A.M.R.1    Norton, E.2    Davison, G.M.3    Babbe, S.M.4    Newell, C.A.5    Gatehouse, J.A.6
  • 17
    • 0001068883 scopus 로고
    • Wound-induced proteinase inhibitor in plant leaves: A possible defense mechanism against insects
    • T.R. Green, and C.A. Ryan Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects Science 175 1972 776 777
    • (1972) Science , vol.175 , pp. 776-777
    • Green, T.R.1    Ryan, C.A.2
  • 18
    • 0032754118 scopus 로고    scopus 로고
    • Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth
    • A.M. Harsulkar, A.P. Giri, A.G. Patankar, V.S. Gupta, M.N. Sainani, P.K. Ranjekar, and V.V. Deshpande Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth Plant Physiol 121 1999 497 506 (Pubitemid 29498911)
    • (1999) Plant Physiology , vol.121 , Issue.2 , pp. 497-506
    • Harsulkar, A.M.1    Giri, A.P.2    Patankar, A.G.3    Gupta, V.S.4    Sainani, M.N.5    Ranjekar, P.K.6    Deshpande, V.V.7
  • 19
    • 0032822646 scopus 로고    scopus 로고
    • Studies on the biological responses of rats to seed trypsin inhibitors using near-isogenic lines of Pisum sativum L (pea)
    • DOI 10.1002/(SICI)1097-0010(199909)79:12<1647::AID-JSFA415>3.0. CO;2-P
    • M. Hedeman, T. Welham, S. Boisen, N. Canibe, L. Bilham, and C. Domoney Studies on the biological responses of rats to seed trypsin inhibitors using nearisogenic lines of Pisum sativum L J Sci Food Agr 79 1999 1647 1653 (Pubitemid 29429081)
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , Issue.12 , pp. 1647-1653
    • Hedemann, M.S.1    Welham, T.2    Boisen, S.3    Canibe, N.4    Bilham, L.5    Domoney, C.6
  • 20
    • 0010268123 scopus 로고
    • Studies on protein fractions and protein quality of buckwheat
    • B. Javornik, B.O. Eggum, and I. Kreft Studies on protein fractions and protein quality of buckwheat Genetika 13 1981 115 121
    • (1981) Genetika , vol.13 , pp. 115-121
    • Javornik, B.1    Eggum, B.O.2    Kreft, I.3
  • 21
    • 59049086814 scopus 로고    scopus 로고
    • Two cell wall Kunitz trypsin inhibitors in chickpea during seed germination and seedling growth
    • H.N. Josefina, M. Ignacio, J. Teresa, D. Berta, and L. Emilia Two cell wall Kunitz trypsin inhibitors in chickpea during seed germination and seedling growth Plant Physiol Biochem 47 2009 181 187
    • (2009) Plant Physiol Biochem , vol.47 , pp. 181-187
    • Josefina, H.N.1    Ignacio, M.2    Teresa, J.3    Berta, D.4    Emilia, L.5
  • 22
    • 0029617837 scopus 로고
    • Purification, characterization, sequence determination, and mass spectrometric analysis of a trypsin inhibitor from seeds of the Brazilian tree Dipteryx alata (Leguminosae)
    • DOI 10.1007/BF01886907
    • D.E. Kalume, M.V. Sousa, and L. Morhy Purification, characterization, sequence determination, and mass spectrometric analysis of a trypsin inhibitor from seeds of the Brazilian tree Dipteryx alata (Leguminosae) J Protein Chem 14 1995 685 693 (Pubitemid 26006117)
    • (1995) Journal of Protein Chemistry , vol.14 , Issue.8 , pp. 685-693
    • Kalume, D.E.1    Sousa, M.V.2    Morhy, L.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • DOI 10.1016/S0167-4838(99)00284-8, PII S0167483899002848
    • M. Laskowski, and M.A. Qasim What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme-substrate complexes Biochim Biophys Acta 1477 2000 324 337 (Pubitemid 30119910)
    • (2000) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1477 , Issue.1-2 , pp. 324-337
    • Laskowski Jr., M.1    Qasim, M.A.2
  • 25
    • 47949098777 scopus 로고    scopus 로고
    • A stable trypsin inhibitor from Chinese dull black soybeans with potentially exploitable activities
    • P. Lin, and T.B. Ng A stable trypsin inhibitor from Chinese dull black soybeans with potentially exploitable activities Process Biochem 43 2008 992 998
    • (2008) Process Biochem , vol.43 , pp. 992-998
    • Lin, P.1    Ng, T.B.2
  • 26
    • 41949092326 scopus 로고    scopus 로고
    • A Kunitz trypsin inhibitor of Entada scandens seeds: Another member with single disulfide bridge
    • M.H. Lingaraju, and L.R. Gowda A Kunitz trypsin inhibitor of Entada scandens seeds: another member with single disulfide bridge Biochim Biophys Acta 1784 2008 850 855
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 850-855
    • Lingaraju, M.H.1    Gowda, L.R.2
  • 28
    • 0034622649 scopus 로고    scopus 로고
    • Trypsin inhibitor from Dimorphandra mollis seeds: Purification and properties
    • DOI 10.1016/S0031-9422(00)00155-2, PII S0031942200001552
    • M.L.R. Macedo, D.G.G. Matos, O.L.T. Machado, S. Marangoni, and J.C. Novello Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties Phytochemistry 54 2000 553 558 (Pubitemid 30625828)
    • (2000) Phytochemistry , vol.54 , Issue.6 , pp. 553-558
    • Macedo, M.L.R.1    De Matos, D.G.G.2    Machado, O.L.T.3    Marangoni, S.4    Novello, J.C.5
  • 29
    • 78149358882 scopus 로고    scopus 로고
    • A novel subclassification for kunitz proteinase inhibitors from Leguminous Seeds
    • L.V.O. Maria, C.C.S. Mariana, C.S. Roberto, V.B. Marlon, and U.S. Misako A novel subclassification for kunitz proteinase inhibitors from Leguminous Seeds Biochimie 92 11 2010 1667 1673
    • (2010) Biochimie , vol.92 , Issue.11 , pp. 1667-1673
    • Maria, L.V.O.1    Mariana, C.C.S.2    Roberto, C.S.3    Marlon, V.B.4    Misako, U.S.5
  • 33
    • 0030237068 scopus 로고    scopus 로고
    • Complete amino acid sequences of two trypsin inhibitors from buckwheat seed
    • DOI 10.1016/0031-9422(96)00311-1, PII S0031942296003111
    • M.J. Pandya, D.A. Smith, A. Yarwood, J. Gilroy, and M. Richardson Complete amino acid sequences of two trypsin inhibitors from buckwheat seed Phytochemistry 43 1996 327 331 (Pubitemid 27065543)
    • (1996) Phytochemistry , vol.43 , Issue.2 , pp. 327-331
    • Pandya, M.J.1    Smith, D.A.2    Yarwood, A.3    Gilroy, J.4    Richardson, M.5
  • 34
    • 0031014216 scopus 로고    scopus 로고
    • Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat (Fagopyrum esculentum Moench)
    • DOI 10.1016/S0014-5793(96)01367-1, PII S0014579396013671
    • S.S. Park, K. Abe, M. Kimura, A. Urisu, and N. Yamasaki Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat (Fagopyrum esculentum Moench) FEBS Lett 400 1997 103 107 (Pubitemid 27046830)
    • (1997) FEBS Letters , vol.400 , Issue.1 , pp. 103-107
    • Park, S.-S.1    Abe, K.2    Kimura, M.3    Urisu, A.4    Yamasaki, N.5
  • 35
    • 76249093070 scopus 로고    scopus 로고
    • Purification and characterization of a Bowman-Birk proteinase inhibitor from the seeds of black gram (Vigna mungo)
    • E.R. Prasad, A. Dutta-Gupta, and K. Padmasree Purification and characterization of a Bowman-Birk proteinase inhibitor from the seeds of black gram (Vigna mungo) Phytochemistry 71 2010 363 372
    • (2010) Phytochemistry , vol.71 , pp. 363-372
    • Prasad, E.R.1    Dutta-Gupta, A.2    Padmasree, K.3
  • 36
    • 77049123441 scopus 로고    scopus 로고
    • Purification, characterization and immunolocalization of a novel protease inhibitor from hemolymph of tasar silkworm, Antheraea mylitta
    • S. Rai, K.K. Aggarwal, B. Mitra, T.K. Das, and C.R. Babu Purification, characterization and immunolocalization of a novel protease inhibitor from hemolymph of tasar silkworm, Antheraea mylitta Peptides 31 2010 474 481
    • (2010) Peptides , vol.31 , pp. 474-481
    • Rai, S.1    Aggarwal, K.K.2    Mitra, B.3    Das, T.K.4    Babu, C.R.5
  • 37
    • 44549085952 scopus 로고    scopus 로고
    • Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds
    • A. Scarafoni, A. Consonni, V. Galbusera, A. Negri, G. Tedeschi, P. Rasmussen, C. Magni, and M. Duranti Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds Phytochemistry 69 2008 1820 1825
    • (2008) Phytochemistry , vol.69 , pp. 1820-1825
    • Scarafoni, A.1    Consonni, A.2    Galbusera, V.3    Negri, A.4    Tedeschi, G.5    Rasmussen, P.6    Magni, C.7    Duranti, M.8
  • 39
    • 0022702370 scopus 로고
    • Purification and characterization of proteinase inhibitors from winged bean (Psophocarpus tetragonolobus (L.) DC.) seeds
    • H. Shibata, S. Hara, T. Ikenaka, and J. Abe Purification and characterization of proteinase inhibitors from winged bean (Psophocarpus tetragonolobus (L.) DC.) seeds J. Biochem 99 1986 1147 1155
    • (1986) J. Biochem , vol.99 , pp. 1147-1155
    • Shibata, H.1    Hara, S.2    Ikenaka, T.3    Abe, J.4
  • 40
    • 0025420171 scopus 로고
    • Monitoring protein cleavage and concurrent disulfide bond assignment using thermospray LC/MS
    • K. Stachowiak, J. Otlewski, A. Polanowski, and D.F. Dyckes Monitoring protein cleavage and concurrent disulfide bond assignment using thermospray LC/MS Peptide Res 3 1990 148 154
    • (1990) Peptide Res , vol.3 , pp. 148-154
    • Stachowiak, K.1    Otlewski, J.2    Polanowski, A.3    Dyckes, D.F.4
  • 41
    • 0041919643 scopus 로고    scopus 로고
    • Protease inhibitors of the sulfonamide type: Anticancer, antiinflammatory, and antiviral agents
    • DOI 10.1002/med.10047
    • C.T. Supuran, A. Casini, and A. Scozzafava Protease inhibitors of the sulfonamide type: anticancer, antiinflammatory, and antiviral agents Med Res Rev 5 2003 535 558 (Pubitemid 37034144)
    • (2003) Medicinal Research Reviews , vol.23 , Issue.5 , pp. 535-558
    • Supuran, C.T.1    Casini, A.2    Scozzafava, A.3
  • 42
    • 31944452028 scopus 로고    scopus 로고
    • High protein buckwheat flour suppresses hypercholesterolemia in rats and gallstone formation in mice by hypercholesterolemic diet and body fat in rats because of its low protein digestibility
    • DOI 10.1016/j.nut.2005.01.012, PII S0899900705003783
    • H. Tomotake, N. Yamamoto, N. Yanaka, H. Ohinata, R. Yamazaki, and J. Kayashita High protein buckwheat flour suppresses hypercholesterolemia in rats and gallstone formation in mice by hypercholesterolemic diet and body fat in rats because of its low protein digestibility Nutrition 22 2006 166 173 (Pubitemid 43188807)
    • (2006) Nutrition , vol.22 , Issue.2 , pp. 166-173
    • Tomotake, H.1    Yamamoto, N.2    Yanaka, N.3    Ohinata, H.4    Yamazaki, R.5    Kayashita, J.6    Kato, N.7
  • 43
    • 2942718871 scopus 로고    scopus 로고
    • New protease inhibitors from buckwheat seeds: Properties, partial amino acid sequences and possible biological role
    • DOI 10.1515/BC.2004.049
    • T. Tsybina, Y. Dunaevsky, A. Musolyamov, T. Egorov, N. Larionova, and M. Belozersky New protease inhibitors from buckwheat seeds: properties, partial amino acid sequences and possible biological role Biol Chem 385 2004 429 434 (Pubitemid 38787123)
    • (2004) Biological Chemistry , vol.385 , Issue.5 , pp. 429-434
    • Tsybina, T.1    Dunaevsky, Y.2    Musolyamov, A.3    Egorov, T.4    Larionova, N.5    Popykina, N.6    Belozersky, M.7
  • 44
    • 0034694798 scopus 로고    scopus 로고
    • Ginkbilobin, a novel antifungal protein from Ginkgo biloba seeds with sequence similarity to embryo-abundant protein
    • DOI 10.1006/bbrc.2000.3929
    • H. Wang, and T. Ginkbilobin A novel antifungal protein from Ginkgo biloba seeds with sequence similarity to embryo-abundant protein Biochem Biophys Res Commun 279 2000 407 411 (Pubitemid 32016730)
    • (2000) Biochemical and Biophysical Research Communications , vol.279 , Issue.2 , pp. 407-411
    • Wang, H.1    Ginkbilobin, T.2
  • 45
    • 35348948452 scopus 로고    scopus 로고
    • Calliandra selloi Macbride trypsin inhibitor: Isolation, characterization, stability, spectroscopic analyses
    • DOI 10.1016/j.phytochem.2007.06.003, PII S0031942207003792
    • L. Yoshizaki, M.F. Troncoso, L.S. Lopes, U. Hellman, L.M. Beltramini, and C.W. Todel Calliandra selloi Macbride trypsin inhibitor: isolation, characterization, stability, spectroscopic analyses Phytochemistry 68 2007 2625 2634 (Pubitemid 47615059)
    • (2007) Phytochemistry , vol.68 , Issue.21 , pp. 2625-2634
    • Yoshizaki, L.1    Troncoso, M.F.2    Lopes, J.L.S.3    Hellman, U.4    Beltramini, L.M.5    Wolfenstein-Todel, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.