Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut. (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Alternative label

• M.Volpicella; J. Cordewener; M.A. Jongsma; R. Gallerani; L.R. Ceci; J. Beekwilder (2006)
  Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut.
  in Journal of chromatography. B (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• M.Volpicella; J. Cordewener; M.A. Jongsma; R. Gallerani; L.R. Ceci; J. Beekwilder (literal)

Pagina inizio

• 26 (literal)

Pagina fine

• 32 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 833 (literal)

Rivista

• Journal of chromatography. B (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• a Department of Biochemistry and Molecular Biology, University of Bari, Via Amendola 165/A, 70126 Bari, Italy b Plant Research International, P.O. box 16, 6700 AA Wageningen, Netherlands c Institute for Biomembranes and Bioenergetic, C.N.R., Trani Unit, Via Corato 17, 70059 Trani, Italy (literal)

Titolo

• Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut. (literal)

Abstract

• Protease inhibitors mediate a natural form of plant defence against insects, by interfering with the digestive system of the insect. In this paper, affinity chromatography was used to isolate trypsins and chymotrypsins from Helicoverpa zea larvae, which had been raised on inhibitor-containing diet. Sensitivity of the fractions to inhibition by plant proteinase inhibitors was tested, and compared to the sensitivity of proteinases found in insects raised on diet to which no inhibitor had been added. The isolated chymotrypsin activity was found to be less sensitive to plant protease inhibitors. The sensitivity of the isolated trypsin activity was found to be intermediate between completely sensitive trypsins and completely insensitive forms that have been previously described. Mass spectrometry was used to identify one trypsin and two chymotrypsins in the partially purified protease fraction. The sequence features of these proteases are discussed in relation to their sensitivity to inhibitors. The results provide insight in the enzymes deployed by Helicoverpa larvae to overcome plant defence. (literal)

Prodotto di

• Istituto di biomembrane e bioenergetica (IBBE) (Istituto)
• Biogenesi delle Membrane di Trasduzione dell'Energia. (SV.P13.002.001) (Modulo)

Autore CNR

• LUIGI RUGGIERO CECI (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut." (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto di biomembrane e bioenergetica (IBBE) (Istituto)
• Biogenesi delle Membrane di Trasduzione dell'Energia. (SV.P13.002.001) (Modulo)

Autore CNR di

• LUIGI RUGGIERO CECI (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of chromatography. B (Rivista)

Insieme di parole chiave di

• Keywords of "Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut." (Insieme di parole chiave)