A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera: Pyralidae)
A 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 tryp...
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| Published in | Biochimica et biophysica acta Vol. 1621; no. 2; pp. 170 - 182 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
02.05.2003
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| Subjects | |
| Online Access | Get full text |
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| Abstract | A 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. |
|---|---|
| AbstractList | A 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 x 10(-10) and 1.6 x 10(-10) M were obtained with bovine and porcine trypsin, respectively. This constant was lower (2.6 x 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 approximately 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 approximately 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.A 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 x 10(-10) and 1.6 x 10(-10) M were obtained with bovine and porcine trypsin, respectively. This constant was lower (2.6 x 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 approximately 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 approximately 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. A 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. A 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 x 10(-10) and 1.6 x 10(-10) M were obtained with bovine and porcine trypsin, respectively. This constant was lower (2.6 x 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 approximately 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 approximately 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. |
| Author | Marangoni, Sérgio Toyama, Marcos H Cabrini, Elaine Cristina Rodrigues Macedo, Maria Lı́gia Machado Freire, Maria das Graças Novello, José Camillo |
| Author_xml | – sequence: 1 givenname: Maria Lı́gia surname: Rodrigues Macedo fullname: Rodrigues Macedo, Maria Lı́gia email: bioplant@terra.com.br organization: Laboratório de Purificação de Proteı́nas e suas Funções Biológicas, Departamento de Ciências Naturais, Universidade Federal de Mato Grosso do Sul, CP 210, CEP 79603-011, Três Lagoas, MS, Brazil – sequence: 2 givenname: Maria das Graças surname: Machado Freire fullname: Machado Freire, Maria das Graças organization: Departamento de Bioquı́mica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), CP 6109, CEP 13093-970, Campinas, SP, Brazil – sequence: 3 givenname: Elaine Cristina surname: Cabrini fullname: Cabrini, Elaine Cristina organization: Laboratório de Purificação de Proteı́nas e suas Funções Biológicas, Departamento de Ciências Naturais, Universidade Federal de Mato Grosso do Sul, CP 210, CEP 79603-011, Três Lagoas, MS, Brazil – sequence: 4 givenname: Marcos H surname: Toyama fullname: Toyama, Marcos H organization: Departamento de Bioquı́mica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), CP 6109, CEP 13093-970, Campinas, SP, Brazil – sequence: 5 givenname: José Camillo surname: Novello fullname: Novello, José Camillo organization: Departamento de Bioquı́mica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), CP 6109, CEP 13093-970, Campinas, SP, Brazil – sequence: 6 givenname: Sérgio surname: Marangoni fullname: Marangoni, Sérgio organization: Departamento de Bioquı́mica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), CP 6109, CEP 13093-970, Campinas, SP, Brazil |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12726993$$D View this record in MEDLINE/PubMed |
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| Keywords | Pest protease Resistance Peltophorum dubium Trypsin inhibitor Anagasta kuehniella |
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| Snippet | A novel trypsin inhibitor was purified from the seeds of
Peltophorum dubium (Spreng.). SDS-PAGE under reducing conditions showed that the inhibitor consisted... A novel trypsin inhibitor was purified from the seeds of Peltophorum dubium (Spreng.). SDS-PAGE under reducing conditions showed that the inhibitor consisted... |
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| SubjectTerms | Amino Acid Sequence Anagasta kuehniella Animals Drug Stability Fabaceae - chemistry Isoelectric Point Lepidoptera - drug effects Lepidoptera - enzymology Molecular Sequence Data Molecular Weight Peltophorum dubium Pest protease Resistance Seeds - chemistry Trypsin inhibitor Trypsin Inhibitors - chemistry Trypsin Inhibitors - isolation & purification Trypsin Inhibitors - pharmacology |
| Title | A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera: Pyralidae) |
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