메뉴 건너뛰기




Volumn 56, Issue 9, 2008, Pages 2989-2995

Antimicrobial, dehydroascorbate reductase, and monodehydroascorbate reductase activities of defensin from sweet potato [Ipomoea batatas (L.) Lam. 'Tainong 57'] storage roots

Author keywords

Antimicrobial activity; Defensin; Dehydroascorbate reductase activity; Gene expression; Monodehydroascorbate reductase activity; Sweet potato

Indexed keywords

ANTIINFECTIVE AGENT; COMPLEMENTARY DNA; DEFENSIN; GLUTATHIONE DEHYDROGENASE (ASCORBATE); MONODEHYDROASCORBATE REDUCTASE; OXIDOREDUCTASE;

EID: 44349167842     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf072994j     Document Type: Article
Times cited : (35)

References (31)
  • 1
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert, W. F.; Terras, F. R. G.; Cammue, B. P. A.; Osborn, R. W. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. 1995, 108, 1353-1358.
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 4
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect R-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat δ-purothionins
    • Bloch, C., Jr.; Richardson, M. A new family of small (5 kDa) protein inhibitors of insect R-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat δ-purothionins. FEBS Lett. 1991, 279, 101-104.
    • (1991) FEBS Lett , vol.279 , pp. 101-104
    • Bloch Jr., C.1    Richardson, M.2
  • 5
    • 0034613541 scopus 로고    scopus 로고
    • Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin
    • Wijaya, R.; Neumann, G. M.; Condron, R.; Hughes, A. B.; Polya, G. M. Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci. 2000, 159, 243-255.
    • (2000) Plant Sci , vol.159 , pp. 243-255
    • Wijaya, R.1    Neumann, G.M.2    Condron, R.3    Hughes, A.B.4    Polya, G.M.5
  • 6
    • 0025080513 scopus 로고
    • α-Purothionins: Amino acid sequence of two polypeptides of new family of thionins from wheat endosperm
    • Colilla, F. J.; Rocher, A.; Mendez, E. α-Purothionins: amino acid sequence of two polypeptides of new family of thionins from wheat endosperm. FEBS Lett. 1990, 270, 191-194.
    • (1990) FEBS Lett , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 7
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, α-hordothionin, from barley endosperm
    • Mendez, E.; Moreno, A.; Colilla, F. J.; Pelaez, F.; Limas, G. G.; Mendez, R. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, α-hordothionin, from barley endosperm. Eur. J. Biochem. 1990, 194, 533-539.
    • (1990) Eur. J. Biochem , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.J.3    Pelaez, F.4    Limas, G.G.5    Mendez, R.6
  • 8
    • 0029014273 scopus 로고
    • Isolation and characterization of plant defensins from seeds of Asteraceae, Hippocastanaceae and Saxifragaceae
    • Osborn, R. W.; De Samblanx, G. W.; Thevissen, K.; Goderis, I.; Torrekens, S.; Van Leuven, F. V. Isolation and characterization of plant defensins from seeds of Asteraceae, Hippocastanaceae and Saxifragaceae. FEBS Lett. 1995, 368, 257-262.
    • (1995) FEBS Lett , vol.368 , pp. 257-262
    • Osborn, R.W.1    De Samblanx, G.W.2    Thevissen, K.3    Goderis, I.4    Torrekens, S.5    Van Leuven, F.V.6
  • 9
    • 0037021614 scopus 로고    scopus 로고
    • A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid
    • Chen, K. C.; Lin, C. Y.; Kuan, C. C.; Sung, H. Y.; Chen, C. S. A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid. J. Agric. Food Chem. 2002, 50, 7258-7263.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 7258-7263
    • Chen, K.C.1    Lin, C.Y.2    Kuan, C.C.3    Sung, H.Y.4    Chen, C.S.5
  • 10
    • 0028271965 scopus 로고    scopus 로고
    • Moreno, M.; Segura, A.; Garcia-Olmedo, F. Pseudothionin-Stl, a potato peptide active against potato pathogens. Eur. J. Biochem. 1994, 223, 135-139.
    • Moreno, M.; Segura, A.; Garcia-Olmedo, F. Pseudothionin-Stl, a potato peptide active against potato pathogens. Eur. J. Biochem. 1994, 223, 135-139.
  • 11
    • 0032436013 scopus 로고    scopus 로고
    • Functional and structural features of δ-zeathionins, a new class of sodium channel blockers
    • Kushmerick, C.; Castro, M. D.; Cruz, J. S.; Bloch, C.; Beirao, P. S. L. Functional and structural features of δ-zeathionins, a new class of sodium channel blockers. FEBS Lett. 1998, 440, 302-306.
    • (1998) FEBS Lett , vol.440 , pp. 302-306
    • Kushmerick, C.1    Castro, M.D.2    Cruz, J.S.3    Bloch, C.4    Beirao, P.S.L.5
  • 13
    • 0001469527 scopus 로고
    • In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to non-specific lipid transfer proteins
    • Terras, F. R.; Goderis, I. J.; Van Leuven, F.; Vanderleyden, J.; Cammue, B. P.; Broekaert, W. F. In vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to non-specific lipid transfer proteins. Plant Physiol. 1992, 100, 1055-1058.
    • (1992) Plant Physiol , vol.100 , pp. 1055-1058
    • Terras, F.R.1    Goderis, I.J.2    Van Leuven, F.3    Vanderleyden, J.4    Cammue, B.P.5    Broekaert, W.F.6
  • 15
    • 0031031792 scopus 로고    scopus 로고
    • ESTs reveal a multigene family for plant defensins in Arabidopsis thaliana
    • Epple, P.; Apel, K. Bohlmann, H. ESTs reveal a multigene family for plant defensins in Arabidopsis thaliana. FEBS Lett. 1997, 400, 168-172.
    • (1997) FEBS Lett , vol.400 , pp. 168-172
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 18
    • 0028519172 scopus 로고
    • Characterization of a predominantly pistil-expressed gene encoding a γ-thionin-like protein of Petunia inflata
    • Karunanandaa, B.; Singh, A.; Kao, T. H. Characterization of a predominantly pistil-expressed gene encoding a γ-thionin-like protein of Petunia inflata. Plant Mol. Biol. 1994, 26, 459-464.
    • (1994) Plant Mol. Biol , vol.26 , pp. 459-464
    • Karunanandaa, B.1    Singh, A.2    Kao, T.H.3
  • 19
    • 33744958482 scopus 로고    scopus 로고
    • Cloning, characterization and antifungal activity of defensin Tfgd1 from Trigonella foenum-graecum L
    • Olli, S.; Kirti, P. B. Cloning, characterization and antifungal activity of defensin Tfgd1 from Trigonella foenum-graecum L. J. Biochem. Mol. Biol. 2006, 39, 278-83.
    • (2006) J. Biochem. Mol. Biol , vol.39 , pp. 278-283
    • Olli, S.1    Kirti, P.B.2
  • 21
    • 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, 680-885.
    • (1970) Nature , vol.227 , pp. 680-885
    • Laemmli, U.K.1
  • 22
    • 0002165231 scopus 로고
    • Level and heat stability of trypsin inhibitor activity among sweet potato (Ipomoea batatas Lam.) varieties
    • Lin, Y. H.; Chen, H. L. Level and heat stability of trypsin inhibitor activity among sweet potato (Ipomoea batatas Lam.) varieties. Bot. Bull. Acad. Sin. 1980, 21, 1-13.
    • (1980) Bot. Bull. Acad. Sin , vol.21 , pp. 1-13
    • Lin, Y.H.1    Chen, H.L.2
  • 25
    • 23244451433 scopus 로고    scopus 로고
    • Expression and localization of protein disulfide isomerase cDNA from sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57') storage roots
    • Huang, D. J.; Chen, H. J.; Hou, W. C.; Lin, Y. H. Expression and localization of protein disulfide isomerase cDNA from sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57') storage roots. Plant Sci. 2005, 169, 776-784.
    • (2005) Plant Sci , vol.169 , pp. 776-784
    • Huang, D.J.1    Chen, H.J.2    Hou, W.C.3    Lin, Y.H.4
  • 26
    • 0002977651 scopus 로고
    • Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions
    • Yamazaki, I.; Pette, L. H. Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions. Biochim. Biophys. Acta 1961, 50, 62-69.
    • (1961) Biochim. Biophys. Acta , vol.50 , pp. 62-69
    • Yamazaki, I.1    Pette, L.H.2
  • 27
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Von Heijne, G. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 1983, 133, 17-21.
    • (1983) Eur. J. Biochem , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 28
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H.; Engelbrecht, J.; Brunak, S.; von Heijne, G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 29
    • 1242277736 scopus 로고    scopus 로고
    • In vitro reduction of trypsin inhibitor by purified NADPH/thioredoxin system from sprouts of sweet potato (Ipomoea batatas (L.) Lam.) storage roots
    • Huang, D. J.; Chen, H. J.; Hou, W. C.; Chen, T. E.; Lin, Y. H. In vitro reduction of trypsin inhibitor by purified NADPH/thioredoxin system from sprouts of sweet potato (Ipomoea batatas (L.) Lam.) storage roots. Plant Sci. 2004, 166, 435-441.
    • (2004) Plant Sci , vol.166 , pp. 435-441
    • Huang, D.J.1    Chen, H.J.2    Hou, W.C.3    Chen, T.E.4    Lin, Y.H.5
  • 30
    • 33750035480 scopus 로고    scopus 로고
    • Dehydroascorbate reductase affects leaf growth, development, and function
    • Chen, Z.; Gallie, D. R. Dehydroascorbate reductase affects leaf growth, development, and function. Plant Physiol. 2006, 42 (2), 775-787.
    • (2006) Plant Physiol , vol.42 , Issue.2 , pp. 775-787
    • Chen, Z.1    Gallie, D.R.2
  • 31
    • 0028136613 scopus 로고
    • A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
    • Trümper, S.; Follmann, H.; Häberlein, I. A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor. FEBS Lett. 1994, 352 (2), 159-162.
    • (1994) FEBS Lett , vol.352 , Issue.2 , pp. 159-162
    • Trümper, S.1    Follmann, H.2    Häberlein, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.