dc.creatorRodrigues Macedo M.L.
dc.creatorFreire M.D.G.M.
dc.creatorCabrini E.C.
dc.creatorToyama M.H.
dc.creatorNovello J.C.
dc.creatorMarangoni S.
dc.date2003
dc.date2015-06-30T17:29:04Z
dc.date2015-11-26T15:41:02Z
dc.date2015-06-30T17:29:04Z
dc.date2015-11-26T15:41:02Z
dc.date.accessioned2018-03-28T22:49:31Z
dc.date.available2018-03-28T22:49:31Z
dc.identifier
dc.identifierBiochimica Et Biophysica Acta - General Subjects. , v. 1621, n. 2, p. 170 - 182, 2003.
dc.identifier3044165
dc.identifier10.1016/S0304-4165(03)00055-2
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0242500472&partnerID=40&md5=f58df18a6f04c217781b0c21315578ff
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/102226
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/102226
dc.identifier2-s2.0-0242500472
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1264519
dc.descriptionA novel trypsin inhibitor was purified from the seeds of Peltophorum dubium (Spreng.). SDS-PAGE under reducing conditions showed that the inhibitor consisted of a single polypeptide chain (ca. 20 kDa). The dissociation constants of 4×10-10 and 1.6×10-10 M were obtained with bovine and porcine trypsin, respectively. This constant was lower (2.6×10-7 M) for chymotrypsin. The inhibitory activity was stable over a wide range of temperature and pH and in the presence of DTT. The N-terminal sequence of the P. dubium inhibitor showed a high degree of homology with other Kunitz-type inhibitors. When fed to the insect Anagasta kuehniella, in an artificial diet (inhibitor concentration 1.6%), the inhibitor produced ∼56% and delayed the development of this lepidopteran. The concentration of inhibitor in the diet necessary to cause a 50% reduction in the weight (ED50) of fourth instar larvae was ∼1%. The action of the P. dubium trypsin inhibitor (PDTI) on A. kuehniella may involve inhibition of the trypsin-like activity present in the larval midgut, resistance of the inhibitor to digestion by midgut enzymes and bovine trypsin, and association of the inhibitor with a chitin column and chitinous structures in the peritrophic membrane and/or midgut of the insect. © 2003 Elsevier Science B.V. All rights reserved.
dc.description1621
dc.description2
dc.description170
dc.description182
dc.descriptionRichardson, M., Seed storage proteins: The enzyme inhibitors (1991) Methods in Plant Biochemistry, Amino Acids, Proteins and Nucleic Acids, 5, pp. 259-305. , Rogers J.L. New York: Academic Press
dc.descriptionRyan, C.A., Protease inhibitors in plants: Genes for improving defenses against insects and pathogens (1990) Annu. Ver. Phytopathol., 28, pp. 425-449
dc.descriptionShewry, P.R., Lucas, J.A., Plant proteins that confer resistance to pests and pathogens (1997) Advances in Botanical Research, 26, pp. 136-192. , Callow J. London: Academic Press
dc.descriptionSouza, E.M.T., Teles, R.C.L., Siqueira, E.M.A., Freitas, S.M., Effects of denaturing and stabilizing agents on the inhibitory activity and conformational stability of Schizolobium parayba chymotrypsin inhibitor (2000) J. Protein Chem., 19, pp. 507-513
dc.descriptionMacedo, M.L.R., Mello, G.C., Freire, M.G.M., Novello, J.C., Marangoni, S., Matos, D.G.G., Effect of a trypsin inhibitor from Dimorphandra mollis seeds on the development of Callosobruchus maculatus (2002) Plant Physiol. Biochem., 40, pp. 891-898
dc.descriptionMacedo, M.L.R., Xavier-Filho, J., Purification and characterization of trypsin inhibitors from seeds of Clitoria ternatea (1992) J. Sci. Food Agric., 58, pp. 55-58
dc.descriptionMello, G.C., Oliva, M.L.V., Sumikawa, J.T., Machado, O.L.T., Marangoni, S., Novello, J.C., Macedo, M.L.R., Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis (2002) J. Protein Chem., 20, pp. 625-632
dc.descriptionOliva, M.L.V., Souza-Pinto, J.C., Batista, I.F.C., Araujo, M.S.A., Silveira, V.F., Auerswald, E.A., Mentele, R., Sampaio, C.A.M., Leucaena leucocephala serine proteinase inhibitor: Primary structure and action on blood coagulation, kinin release and rat paw edema (2000) Biochim. Biophys. Acta, 1477, pp. 64-74
dc.descriptionBirk, Y., Protein proteinase inhibitors in legume seeds - Overview (1994) Arch. Latinoam. Nutr., 44, pp. 26-30
dc.descriptionJohnston, K.A., Lee, M., Brough, C., Hilder, V.A., Gatehouse, A.M.R., Gatehouse, J.A., Protease activities in the larval midgut of Heliothis virescens: Evidence for trypsin and chymotrypsin-like enzymes (1995) Insect Biochem. Mol. Biol., 25, pp. 375-383
dc.descriptionChristeller, J.T., Laing, W.A., Marwick, N.P., Burges, E.P.J., Midgut protease activities in 12 phytophagous lepidopteran larvae: Dietary and protease inhibitor interactions (1992) Insect Biochem. Mol. Biol., 22, pp. 735-746
dc.descriptionDe Leo, F., Bonadé-Bottino, M., Ceci, L.R., Gallerani, R., Joaunin, L., Effects of a mustard trypsin inhibitor expressed in different plants on three lepidopteran pests (2001) Insect Biochem. Mol. Biol., 31, pp. 593-602
dc.descriptionHilder, V.A., Gatehouse, A.M.R., Sheerman, S.E., Barker, R.F., Boulter, D., A novel mechanism of insect resistance engineered into tobacco (1987) Nature, 330, pp. 160-163
dc.descriptionMcManus, M.T., White, D.W.R., McGragor, P.G., Accumulation of a chymotrypsin inhibitor in transgenic tobacco can affect the growth of insect pests (1994) Transgenic Res., 3, pp. 50-58
dc.descriptionYeh, K.W., Lin, M.I., Tuan, S.J., Chen, Y.M., Lin, C.Y., Kao, S.S., Sweet potato (Ipomea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura (1997) Plant Cell Rep., 16, pp. 696-699
dc.descriptionLeplé, J.C., Bonadé-Bottino, M., Augustin, S., Pilate, G., Dumanois-Le, T.V., Delplanque, A., Cornu, D., Jouanin, L., Toxicity to Chrysomela tremulae (Coleoptera: Chrysomelidae) of transgenic poplars expressing a cysteine proteinase inhibitor (1995) Mol. Breed., 1, pp. 319-328
dc.descriptionLecardonnel, A., Chauvin, L., Joaunin, L., Beaujean, A., Prevost, G., Sangwan-Norreel, B., Effects of rice cystatin I expression in transgenic potato on Colorado potato beetle larvae (1999) Plant Sci., 140, pp. 71-79
dc.descriptionGatehouse, A.M.R., Norton, E., Davison, G.M., Babbé, S.M., Newell, C.A., Gatehouse, J.A., Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleraceae
dc.descriptionEffects of plant protease inhibitors in vitro and in vivo (1999) J. Insect Physiol., 45, pp. 545-558
dc.descriptionJouanin, L., Bonadé-Bottino, M., Girard, C., Morrot, G., Giband, M., Transgenic plants for insect resistance (1998) Plant Sci., 131, pp. 1-11
dc.descriptionGatehouse, A.M.R., Gatehouse, J.R., Identifying proteins with insecticidal activity: Use of encoding genes to produce insect-resistant transgenic crops (1998) Pestic. Sci., 52, pp. 165-175
dc.descriptionReckel, G.R.K., Kramer, K.J., Baker, J.E., Kanost, M.R., Fabrick, J.A., Behnke, G.A., Proteinase inhibitors and resistance of transgenic plants to insects (1997) Advances in Insect Control. The Role of Transgenic Plants, pp. 157-183. , N. Carozzi, & M. Koziel. London: Taylor and Francis
dc.descriptionOrtego, F., Novillo, C., Castañera, P., Characterization and distribution of digestive proteases of the salk corn borer, Sesamia nonagrioides Lef. (Lepidoptera: Noctuidae) (1996) Arch. Insect Biochem. Physiol., 33, pp. 163-180
dc.descriptionBroadway, R.M., Dietary proteinase inhibitors alter the complement of midgut proteinases (1996) Arch. Insect Biochem., 41, pp. 107-116
dc.descriptionWu, Y., Llewllyn, D., Matthews, A., Dennis, E.S., Adaptation of Helicoverpa armigera (Lepidoptera: Noctuidaea) to a proteinase inhibitor expressed in transgenic tobacco (1997) Mol. Breed., 3, pp. 371-380
dc.descriptionGiri, A.P., Harsulkar, A.M., Desphande, V.V., Sainani, M.N., Gupta, V.S., Ranjekar, P.K., Chickpea defensive proteinase inhibitors can be inactivated by podborer gut proteinases (1998) Plant Physiol., 116, pp. 393-401
dc.descriptionGirard, C., Le Métayer, M., Bonadé-Bottino, M., Pham-Delegue, M.H., Jouanin, L., A high level of resistance to proteinase inhibitors may be conferred by proteolytic cleavage in beetle larvae (1998) Insect Biochem. Mol. Biol., 28, pp. 229-237
dc.descriptionXavier-Filho, J., Campos, F.A.P., Ary, M.B., Silva, C.P., Carvalho, M.M.M., Macedo, M.L.R., Lemos, F.J.A., Grant, G., Poor correlation between the levels of proteinase inhibitors found in seeds of different cultivars of cowpea (Vigna unguiculata) and the resistance/susceptibility to predation by Callosobruchus maculatus (1989) J. Agric. Food Chem., 37, pp. 1139-1143
dc.descriptionBernfield, P., Amylases, α and β (1955) Methods in Enzymology, pp. 149-158. , S.P. Collowick, & N.O. Kaplan. New York: Academic Press
dc.descriptionBradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
dc.descriptionLaemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage (1970) Nature, 227, pp. 680-685
dc.descriptionWestermeier, R., Gel Electrophoresis (1993) A Guide to Theory and Practice, pp. 210-212. , H.F. Ebel. New York: VCH Publishers
dc.descriptionUriel, J., Berges, J., Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis in acrylamide-agarose gels (1968) Nature, 218, pp. 578-580
dc.descriptionKnight, C.G., The characterization of enzyme inhibition (1986) Proteinase Inhibitors, pp. 23-51. , A.J. Barret, & G. Salvesen. Amsterdam: Elsevier
dc.descriptionLiu, W.W., Feinstein, G., Osuga, D.T., Haynes, D.T., Feeney, R.E., Modification or arginines in trypsin inhibitors by 1,2-cyclohexanedione (1968) Biochemistry, 7, pp. 2886-2892
dc.descriptionKunitz, M., Crystalline soybean trypsin inhibitor. Part II: General properties (1945) J. Gen. Physiol., 30, pp. 291-310
dc.descriptionHenrison, R.L., Meredith, S.C., Amino acid analysis by reverse phase high performance liquid chromatoghraphy: Precolumn derivatization with phenyliosothiocyanate (1984) Anal. Biochem., 136, pp. 65-71
dc.descriptionHowe, R.W., A parameter for expressing the suitability of an environment for insect development (1971) J. Stored Prod. Res., 7, pp. 63-65
dc.descriptionJoubert, F.J., Purification and some properties of a proteinase inhibitor (DE-1) from Peltophorum africanum (weeping wattle) seed (1981) Hoppe-Seyler Z. Physiol. Chem., 362, pp. 1515-1521
dc.descriptionOdani, S., Ikenaka, T., Studies on soybean trypsin inhibitors: XI complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor C-II (1977) J. Biochem., 82, pp. 1523-1531
dc.descriptionTerada, S., Fujimura, S., Kino, S., Kimoto, E., Purification and characterization of three proteinase inhibitors from Canavalia lineata seeds (1994) Biosci. Biotechnol. Biochem., 58, pp. 371-375
dc.descriptionLin, G., Bode, W., Huber, R., Chi, C., Engh, R.A., The 0.25 nm X-ray structure of the Bowman-Birk inhibitor from mung bean in ternary complex with porcine trypsin (1993) Eur. J. Biochem., 212, pp. 549-555
dc.descriptionKortt, A.A., Jermyn, M.A., Acacia proteinase inhibitors. Purification and properties of the trypsin inhibitors from Acacia elata seed (1981) Eur. J. Biochem., 115, pp. 551-557
dc.descriptionRichardson, M., Campos, F.A.P., Xavier-Filho, J., Macedo, M.L.R., Maia, G.M.C., Yarwood, A., The amino acid sequence and reactive (inhibitory) site of the major trypsin isoinhibitor (DE5) isolated from seeds of the Brazilian Carolina tree (Adenanthera pavonina L.) (1986) Biochim. Biophys. Acta, 872, pp. 134-140
dc.descriptionKoide, T., Ikenaka, T., Studies on soybean trypsin inhibitors: 3. Amino-acid sequences of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz) (1973) Eur. J. Biochem., 32, pp. 417-431
dc.descriptionMichaud, D., Avoiding protease-mediated resistance in herbivorous pests (1997) Trends Biotechnol., 15, pp. 4-6
dc.descriptionDuan, X., Li, X., Xue, Q., Abo-El-Saad, M., Xu, R., Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant (1996) Nat. Biotechnol., 14, pp. 494-498
dc.descriptionJoubert, F.J., Kruger, H., Townshed, G.S., Botes, D.P., Purification, some properties and the complete primary structure of two protease inhibitors (DE-5 and DE-4) from Macrotyloma axillare seed (1979) Eur. J. Biochem., 97, pp. 85-91
dc.descriptionYamamoto, M., Hara, S., Ikenaka, T., Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L) DC) (1983) J. Biochem., 94, pp. 849-863
dc.descriptionMacedo, M.L.R., Matos, D.G.G., Machado, O.L.T., Marangoni, S., Novello, J.C., Trypsin inhibitor from Dimorphandra mollis seeds: Purification and properties (2000) Phytochemistry, 54, pp. 553-558
dc.descriptionNorioka, N., Hara, S., Ikenaka, T., Abe, J., Distribution of the Kunitz and the Bowman-Birk family proteinase inhibitors in leguminous seeds (1988) Agric. Biol. Chem., 52, pp. 1245-1252
dc.descriptionSouza, E.M.T., Mizuta, K., Sampaio, U.M., Sampaio, C.A.M., Purification and partial characterization of a Schizolobium parayba chymotrypsin inhibitor (1995) Phytochemistry, 39, pp. 521-525
dc.descriptionBatista, I.F.C., Oliva, M.L.V., Araujo, M.A., Sampaio, M.U., Richardson, M., Fritz, H., Sampaio, C.A.M., Primary structure of a Kunitz trypsin inhibitor from Enterolobium contortisiliquum seeds (1996) Phytochemistry, 4, pp. 1017-1022
dc.descriptionRamasarma, P.R., Rao, A.G.A., Rao, R.R., Role of disulfide linkages in structure and activity of proteinase inhibitor from horsegram (Dolichos biflours) (1995) Biochim. Biophys. Acta, 1248, pp. 35-42
dc.descriptionLehle, K., Konert, U., Stern, A., Popp, A., Jaenicke, R., Effect of disulfide bonds on the structure, function, and stability of the trypsin/tPA inhibitor from Erythrina caffra: Site-directed mutagenesis, expression, and physiochemical characterization (1996) Nat. Biotechnol., 14, pp. 476-480
dc.descriptionOliva, M.L.V., Santomauro-Vaz, E.M., Andrade, A.S., Juliano, M.A., Pott, V.J., Sampaio, U.M., Sampaio, C.A.M., Synthetic peptides and fluorogenic substrates related to the reactive site sequence of Kunitz-type inhibitors isolated from Bauhinia: Interaction with human plasma kallikrein (2001) J. Biol. Chem., 383, pp. 109-113
dc.descriptionHabeeb, A.F.S.A., Determination of three amino groups in protein by trinitrobenzenesulfonic acid (1996) Anal. Biochem., 14, pp. 328-336
dc.descriptionTerra, W.R., Ferreira, C., Insect digestive enzymes: Properties, compartmentalization and function (1994) Comp. Biochem. Physiol., 109 B, pp. 1-62
dc.descriptionJongsma, M., Bolter, C., The adaptation of insects to plant protease inhibitors (1997) J. Insect Physiol., 43, pp. 885-895
dc.descriptionBurgess, E.P.J., Malone, L.A., Christeller, J.T., Effects of two proteinase inhibitors on the digestive enzymes and survival of honey bees (Apis mellifera) (1996) J. Insect Physiol., 42, pp. 823-828
dc.descriptionHealth, R.L., Mcdonald, G., Christeller, J.T., Lee, M., Bateman, K., West, J., Heeswijck, R.V., Anderson, M.A., Protease inhibitors from Nicotiana alata enhance plant resistance to insect pests (1997) J. Insect Physiol., 43, pp. 833-842
dc.descriptionSchroerder, H.E., Gollasch, S., Moore, A., Tabe, L.M., Craig, S., Hardie, D.C., Chrispeels, M.J., Higgins, T.J.V., Bean α-amylase inhibitor confers resistance to the pea weevil (Bruchus pisorum) in transgenic peas (Pisum sativum L.) (1995) Plant Physiol., 107, pp. 1233-1239
dc.descriptionIshimoto, M., Chrispeels, M.J., Protective mechanism of the Mexican bean weevil against high levels of α-amylase inhibitor in the common bean (1996) Plant Physiol., 111, pp. 393-401
dc.descriptionMacedo, M.L.R., Coelho, M.B., Freire, M.G.M., Machado, O.L.T., Marangoni, S., Novello, J.C., Effect of a toxic protein isolated from Zea mays seeds on the development and survival of the cowpea weevil, Callosobruchus maculatus (2000) Prot. Peptide Letters, 17, pp. 25-31
dc.descriptionVisal, S., Taylor, M.A.J., Michaud, D., The proregion of papaya proteinsae IV inhibits Colorado potato beetle digestive cysteine proteinases (1998) FEBS Lett., 434, pp. 401-405
dc.descriptionMacedo, M.L.R., Fernandes, K.V.S., Sales, M.P., Xavier-Filho, J., Vicilin variants and the resistance of cowpea (Vigna unguiculata) seeds to the cowpea weevil (Callosobruchus maculatus) (1993) Comp. Biochem. Physiol., 105 C, pp. 89-94
dc.descriptionTellam, R.L., Wijffels, G., Willadsen, P., Peritrophic matrix proteins (1999) Insect Biochem. Mol. Biol., 29, pp. 87-101
dc.descriptionMacedo, M.L.R., Fernandes, K.V.S., Sales, M.P., Xavier-Filho, J., Purification and properties of storage proteins (vicilins) from cowpea (Vigna unguiculata) seeds which are susceptible of resistance to the Bruchidae beetle Callosobruchus maculatus (1995) Braz. J. Med. Biol. Res., 28, pp. 183-189
dc.descriptionSales, M.P., Pimenta, P.P., Paes, N.S., Grossi-de-Sa, M.F., Xavier-Filho, J., Vicilins (7S storage globulins) of cowpea (Vigna unguiculata) seeds bind to chitinous structures of the midgut of Callosobruchus maculatus (Coleoptera: Bruchidae) larvae (2001) Braz. J. Med. Biol. Res., 34, pp. 27-34
dc.descriptionRichards, P.A., The peritrophic membranes of insects (1977) Annu. Rev. Entomol., 22, pp. 219-240
dc.languageen
dc.publisher
dc.relationBiochimica et Biophysica Acta - General Subjects
dc.rightsfechado
dc.sourceScopus
dc.titleA Trypsin Inhibitor From Peltophorum Dubium Seeds Active Against Pest Proteases And Its Effect On The Survival Of Anagasta Kuehniella (lepidoptera: Pyralidae)
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución