메뉴 건너뛰기




Volumn 52, Issue 1, 2009, Pages 27-34

Biochemistry of nectar proteins

Author keywords

Hydrogen peroxide; Nectar protein; Nectarin; Nectary; Redox cycle

Indexed keywords


EID: 70349426155     PISSN: 12269239     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12374-008-9007-5     Document Type: Review
Times cited : (38)

References (42)
  • 1
    • 0023897899 scopus 로고
    • Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: Subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase
    • Ahmad S, Pritsos C, Bowen S, Heisler C, Blomquist G, Pardini R (1988) Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase. Free Radic Res Commun 4:403-408
    • (1988) Free Radic Res Commun , vol.4 , pp. 403-408
    • Ahmad, S.1    Pritsos, C.2    Bowen, S.3    Heisler, C.4    Blomquist, G.5    Pardini, R.6
  • 2
    • 0032715514 scopus 로고    scopus 로고
    • Antimicrobial properties of allicin from garlic
    • Ankri S, Mirelman D (1999) Antimicrobial properties of allicin from garlic. Microbes Infect 1(2):125-129
    • (1999) Microbes Infect , vol.1 , Issue.2 , pp. 125-129
    • Ankri, S.1    Mirelman, D.2
  • 3
    • 0030765775 scopus 로고    scopus 로고
    • Allicin from garlic strongly inhibits cysteine proteinases and cytopathic effects of Entamoeba histolytica
    • Ankri S, Miron T, Rabinkov A, Wilchek M, Mirelman D (1997) Allicin from garlic strongly inhibits cysteine proteinases and cytopathic effects of Entamoeba histolytica. Antimicrob Agents Chemother 41(10):2286-2288
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.10 , pp. 2286-2288
    • Ankri, S.1    Miron, T.2    Rabinkov, A.3    Wilchek, M.4    Mirelman, D.5
  • 4
    • 0023442484 scopus 로고
    • Peroxisomes in wild-type and rosy mutant Drosophila melanogaster
    • Beard M, Holtzman E (1987) Peroxisomes in wild-type and rosy mutant Drosophila melanogaster. Proc Natl Acad Sci U S A 84:7433-7437
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7433-7437
    • Beard, M.1    Holtzman, E.2
  • 5
    • 0037483055 scopus 로고    scopus 로고
    • The nectary is the primary site of infection by Erwinia amylovora (Burr.) Winslow et al.: A minireview
    • Bubán T, Orosz-Kovács Z, Farkas Á (2003) The nectary is the primary site of infection by Erwinia amylovora (Burr.) Plant Syst Evol 238:183-194
    • (2003) Plant Syst Evol , vol.238 , pp. 183-194
    • Bubán, T.1    Orosz-Kovács, Z.2    Farkas, Á.3
  • 6
    • 0032435630 scopus 로고    scopus 로고
    • Arabidopsis thaliana contains a large family of germin-like proteins: Characterization of cDNA and genomic sequences encoding 12 unique family members
    • Carter C, Graham R, Thornburg RW (1998) Arabidopsis thaliana contains a large family of germin-like proteins: characterization of cDNA and genomic sequences encoding 12 unique family members. Plant Mol Biol 38:929-943
    • (1998) Plant Mol Biol , vol.38 , pp. 929-943
    • Carter, C.1    Graham, R.2    Thornburg, R.W.3
  • 7
    • 0033197629 scopus 로고    scopus 로고
    • Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp
    • Carter C, Graham R, Thornburg RW (1999) Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp. Plant Mol Biol 41:207-216
    • (1999) Plant Mol Biol , vol.41 , pp. 207-216
    • Carter, C.1    Graham, R.2    Thornburg, R.W.3
  • 8
    • 33846391335 scopus 로고    scopus 로고
    • Tobacco nectaries express a novel NADPH oxidase that is implicated in the defense of floral reproductive tissues against microorganisms
    • Carter C, Healy R, O'Tool NM, Naqvi SMS, Ren G, Park S, Beattie GA, Horner HT, Thornburg RW (2007) Tobacco nectaries express a novel NADPH oxidase that is implicated in the defense of floral reproductive tissues against microorganisms. Plant Physiol 143:389-399
    • (2007) Plant Physiol , vol.143 , pp. 389-399
    • Carter, C.1    Healy, R.2    O'Tool, N.M.3    Naqvi, S.M.S.4    Ren, G.5    Park, S.6    Beattie, G.A.7    Horner, H.T.8    Thornburg, R.W.9
  • 9
    • 0002939333 scopus 로고    scopus 로고
    • Germin-like proteins: Structure, phylogeny and function
    • Carter C, Thornburg RW (1999) Germin-like proteins: structure, phylogeny and function. J Plant Biol 42:97-108
    • (1999) J Plant Biol , vol.42 , pp. 97-108
    • Carter, C.1    Thornburg, R.W.2
  • 10
    • 0034711245 scopus 로고    scopus 로고
    • Tobacco Nectarin I: Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues
    • Carter C, Thornburg RW (2000) Tobacco Nectarin I: purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues. J Biol Chem 275:36726-36733
    • (2000) J Biol Chem , vol.275 , pp. 36726-36733
    • Carter, C.1    Thornburg, R.W.2
  • 11
    • 0037339667 scopus 로고    scopus 로고
    • The nectary-specific pattern of gene expression is regulated by multiple promoter elements in the tobacco Nectarin I promoter
    • Carter C, Thornburg RW (2003) The nectary-specific pattern of gene expression is regulated by multiple promoter elements in the tobacco Nectarin I promoter. Plant Mol Biol 51:451-457
    • (2003) Plant Mol Biol , vol.51 , pp. 451-457
    • Carter, C.1    Thornburg, R.W.2
  • 12
    • 3042835494 scopus 로고    scopus 로고
    • Tobacco Nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities
    • Carter C, Thornburg RW (2004a) Tobacco Nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities. Plant Mol Biol 54:415-425
    • (2004) Plant Mol Biol , vol.54 , pp. 415-425
    • Carter, C.1    Thornburg, R.W.2
  • 13
    • 0842264011 scopus 로고    scopus 로고
    • Tobacco Nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity
    • Carter C, Thornburg RW (2004b) Tobacco Nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity. Plant Physiol 134:460-469
    • (2004) Plant Physiol , vol.134 , pp. 460-469
    • Carter, C.1    Thornburg, R.W.2
  • 14
    • 0029310607 scopus 로고
    • Isolation and characterization of cDNA clones representing the genes encoding the major tuber storage protein (dioscorin) of yam (Dioscorea cayenensis Lam.)
    • Conlan RS, Griffiths LA, Napier JA, Shewry PR, Mantell S, Ainsworth C (1995) Isolation and characterization of cDNA clones representing the genes encoding the major tuber storage protein (dioscorin) of yam (Dioscorea cayenensis Lam.). Plant Mol Biol 28(3):369-380
    • (1995) Plant Mol Biol , vol.28 , Issue.3 , pp. 369-380
    • Conlan, R.S.1    Griffiths, L.A.2    Napier, J.A.3    Shewry, P.R.4    Mantell, S.5    Ainsworth, C.6
  • 15
    • 0031615808 scopus 로고    scopus 로고
    • Peroxidase activity in Malpighian tubules of Triatoma infestans Klug
    • de Azeredo-Oliveira M, Mello M (1998) Peroxidase activity in Malpighian tubules of Triatoma infestans Klug. Cytobios 93:83-92
    • (1998) Cytobios , vol.93 , pp. 83-92
    • de Azeredo-Oliveira, M.1    Mello, M.2
  • 16
    • 0025751609 scopus 로고
    • Molecular cloning, expression and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack
    • Dittrich H, Kutchan TM (1991) Molecular cloning, expression and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc Natl Acad Sci U S A 88:9969-9973
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9969-9973
    • Dittrich, H.1    Kutchan, T.M.2
  • 17
    • 0029294599 scopus 로고
    • Three glycosylated polypeptides secreted by several embryogenic cell cultures of pine show highly specific serological affinity to antibodies directed against the wheat germin apoprotein monomer
    • Domon J-M, Dumas B, Lainé E, Meyer Y, Alain D, David H (1995) Three glycosylated polypeptides secreted by several embryogenic cell cultures of pine show highly specific serological affinity to antibodies directed against the wheat germin apoprotein monomer. Plant Physiol 108:141-148
    • (1995) Plant Physiol , vol.108 , pp. 141-148
    • Domon, J.-M.1    Dumas, B.2    Lainé, E.3    Meyer, Y.4    Alain, D.5    David, H.6
  • 19
    • 0031979636 scopus 로고    scopus 로고
    • Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase
    • Gane PJ, Dunwell JM, Warwicker J (1998) Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase. J Mol Evol 46:488-493
    • (1998) J Mol Evol , vol.46 , pp. 488-493
    • Gane, P.J.1    Dunwell, J.M.2    Warwicker, J.3
  • 21
    • 0033521146 scopus 로고    scopus 로고
    • Dioscorins, the major tuber storage proteins of yam (Dioscorea batatas Decne), with dehydroascorbate reductase and monodehydroascorbate reductase activities
    • Hou W, Chen H, Lin Y (1999) Dioscorins, the major tuber storage proteins of yam (Dioscorea batatas Decne), with dehydroascorbate reductase and monodehydroascorbate reductase activities. Plant Sci 149:151-156
    • (1999) Plant Sci , vol.149 , pp. 151-156
    • Hou, W.1    Chen, H.2    Lin, Y.3
  • 22
    • 0032841621 scopus 로고    scopus 로고
    • Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities
    • Hou W, Liu J, Chen H, Chen T, Chang C, Lin Y (1999) Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities. J Agric Food Chem 5:2168-2172
    • (1999) J Agric Food Chem , vol.5 , pp. 2168-2172
    • Hou, W.1    Liu, J.2    Chen, H.3    Chen, T.4    Chang, C.5    Lin, Y.6
  • 23
    • 0034780180 scopus 로고    scopus 로고
    • Antioxidant activities of dioscorin, the storage protein of yam (Dioscorea batatas Decne) tuber
    • Hou W, Lee MH, Chen H, Liang W, Han CH, Liu YW, Lin YH (2001) Antioxidant activities of dioscorin, the storage protein of yam (Dioscorea batatas Decne) tuber. J Agric Food Chem 49(10):4956-4960
    • (2001) J Agric Food Chem , vol.49 , Issue.10 , pp. 4956-4960
    • Hou, W.1    Lee, M.H.2    Chen, H.3    Liang, W.4    Han, C.H.5    Liu, Y.W.6    Lin, Y.H.7
  • 24
    • 0014962945 scopus 로고
    • Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme
    • Keele BJ, McCord J, Fridovich I (1970) Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme. J Biol Chem 245:6176-6181
    • (1970) J Biol Chem , vol.245 , pp. 6176-6181
    • Keele, B.J.1    McCord, J.2    Fridovich, I.3
  • 25
    • 0025198745 scopus 로고
    • The degree of susceptibility of nectary-inoculated cotton flowers and bolls to subsequent seed infection by Aspergillus flavus is determined at or before anthesis
    • Klich MA (1990) The degree of susceptibility of nectary-inoculated cotton flowers and bolls to subsequent seed infection by Aspergillus flavus is determined at or before anthesis. Appl Environ Microbiol 56(8):2499-2502
    • (1990) Appl Environ Microbiol , vol.56 , Issue.8 , pp. 2499-2502
    • Klich, M.A.1
  • 26
    • 0343514710 scopus 로고
    • Field studies on the mode of entry of Aspergillus flavus into cotton seeds
    • Klich MA, Thomas SH, Mellon JE (1984) Field studies on the mode of entry of Aspergillus flavus into cotton seeds. Mycologia 76:665-669
    • (1984) Mycologia , vol.76 , pp. 665-669
    • Klich, M.A.1    Thomas, S.H.2    Mellon, J.E.3
  • 27
    • 0037195953 scopus 로고    scopus 로고
    • The active principle of garlic at atomic resolution
    • Kuettner EB, Hilgenfeld R, Weiss MS (2002) The active principle of garlic at atomic resolution. J Biol Chem 277(48):46402-46407
    • (2002) J Biol Chem , vol.277 , Issue.48 , pp. 46402-46407
    • Kuettner, E.B.1    Hilgenfeld, R.2    Weiss, M.S.3
  • 28
    • 0027161641 scopus 로고
    • Germin, a protein marker of early plant development is an oxalate oxidase
    • Lane BG, Dunwell JM, Ray JA, Schmitt MR, Cuming AC (1993) Germin, a protein marker of early plant development is an oxalate oxidase. J Biol Chem 268(17):12239-12242
    • (1993) J Biol Chem , vol.268 , Issue.17 , pp. 12239-12242
    • Lane, B.G.1    Dunwell, J.M.2    Ray, J.A.3    Schmitt, M.R.4    Cuming, A.C.5
  • 30
    • 84920181125 scopus 로고    scopus 로고
    • Nectar chemistry
    • E. Pacini, M. Nepi, and S. Nicolson (Eds.), Amsterdam: Springer
    • Nicolson S, Thornburg RW (2007) Nectar chemistry. In: Pacini E, Nepi M, Nicolson S (eds) Nectary and nectar: a modern treatise. Springer, Amsterdam, pp 215-263
    • (2007) Nectary and Nectar: A Modern Treatise , pp. 215-263
    • Nicolson, S.1    Thornburg, R.W.2
  • 33
    • 0030903904 scopus 로고    scopus 로고
    • Lectin and alliinase are the predominant proteins in nectar from leek (Allium porrum L.) flowers
    • Peumans WJ, Smeets K, van Nerum K, van Leuven F, van Damme EJM (1997) Lectin and alliinase are the predominant proteins in nectar from leek (Allium porrum L.) flowers. Planta 201:298-302
    • (1997) Planta , vol.201 , pp. 298-302
    • Peumans, W.J.1    Smeets, K.2    van Nerum, K.3    van Leuven, F.4    van Damme, E.J.M.5
  • 36
  • 37
    • 0028814176 scopus 로고
    • Toxicity of lectins and processing of ingested proteins in the pea aphid Acyrthosiphon pisum
    • Rabhé Y, Sauvion N, Febvay G, Peumans W, Gatehouse A (1995) Toxicity of lectins and processing of ingested proteins in the pea aphid Acyrthosiphon pisum. Entomol Exp Appl 76:143-155
    • (1995) Entomol Exp Appl , vol.76 , pp. 143-155
    • Rabhé, Y.1    Sauvion, N.2    Febvay, G.3    Peumans, W.4    Gatehouse, A.5
  • 39
    • 0016264038 scopus 로고
    • Bovine erythrocyte superoxide dismutase. Complete amino acid sequence
    • Steinman H, Naik V, Abernethy J, Hill R (1974) Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J Biol Chem 249:7326-7338
    • (1974) J Biol Chem , vol.249 , pp. 7326-7338
    • Steinman, H.1    Naik, V.2    Abernethy, J.3    Hill, R.4
  • 41
    • 0033584947 scopus 로고    scopus 로고
    • Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata
    • Yamahara T, Shiono Y, Suzuki T, Tanaka K, Takio S, Sato K, Yamazaki S, Satoh T (1999) Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata. J Biol Chem 274:33274-33278
    • (1999) J Biol Chem , vol.274 , pp. 33274-33278
    • Yamahara, T.1    Shiono, Y.2    Suzuki, T.3    Tanaka, K.4    Takio, S.5    Sato, K.6    Yamazaki, S.7    Satoh, T.8
  • 42
    • 0015903497 scopus 로고
    • An iron-containing superoxide dismutase from Escherichia coli
    • Yost FJ, Fridovich I (1973) An iron-containing superoxide dismutase from Escherichia coli. J Biol Chem 248:4905-4908
    • (1973) J Biol Chem , vol.248 , pp. 4905-4908
    • Yost, F.J.1    Fridovich, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.