A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera : Pyralidae)

dc.creatorMacedo, MLR
dc.creatorFreire, MDM
dc.creatorCabrini, EC
dc.creatorToyama, MH
dc.creatorNovello, JC
dc.creatorMarangoni, S
dc.date2003
dc.dateMAY 2
dc.date2014-11-16T22:42:52Z
dc.date2015-11-26T17:27:02Z
dc.date2014-11-16T22:42:52Z
dc.date2015-11-26T17:27:02Z
dc.date.accessioned2018-03-29T00:14:11Z
dc.date.available2018-03-29T00:14:11Z
dc.identifierBiochimica Et Biophysica Acta-general Subjects. Elsevier Science Bv, v. 1621, n. 2, n. 170, n. 182, 2003.
dc.identifier0304-4165
dc.identifierWOS:000182789100006
dc.identifier10.1016/S0304-4165(03)00055-2
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/53943
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/53943
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/53943
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1284697
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 4x10(-10) and 1.6x10(-10) M were obtained with bovine and porcine trypsin, respectively. This constant was lower (2.6x10(-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 similar to56% 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 similar to1%. 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. (C) 2003 Elsevier Science B.V. All rights reserved.
dc.description1621
dc.description2
dc.description170
dc.description182
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationBiochimica Et Biophysica Acta-general Subjects
dc.relationBiochim. Biophys. Acta-Gen. Subj.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjecttrypsin inhibitor
dc.subjectAnagasta kuehniella
dc.subjectPeltophorum dubium
dc.subjectpest protease
dc.subjectresistance
dc.subjectCowpea Vigna-unguiculata
dc.subjectAmino-acid Sequence
dc.subjectDimorphandra-mollis Seeds
dc.subjectAlpha-amylase Inhibitor
dc.subjectProteinase-inhibitors
dc.subjectCallosobruchus-maculatus
dc.subjectTransgenic Tobacco
dc.subjectChymotrypsin Inhibitor
dc.subjectInsect Resistance
dc.subjectBeetle Larvae
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


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