PoplarV1, Main, Exploration, bibRecord, 003689

Characterization of a saccharide-binding protein from Talisia esculenta seeds with trypsin inhibitory activity.

Identifieur interne : 003689 ( Main/Exploration ); précédent : 003688; suivant : 003690

Characterization of a saccharide-binding protein from Talisia esculenta seeds with trypsin inhibitory activity.

Auteurs : Maria Das Graças M. Freire [Brésil] ; Ilka Maria Vasconcelos ; Marcos Vinïcius Oliveira ; Gonçalo Apolinário De Souza Filho ; Maria Lïgia R. Macedo

Source :

Protein and peptide letters [ 1875-5305 ] ; 2009.

RBID : pubmed:20001918

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Molecular Sequence Data (MeSH), Receptors, Cell Surface (chemistry), Receptors, Cell Surface (genetics), Receptors, Cell Surface (metabolism), Sapindaceae (genetics), Sapindaceae (metabolism), Seeds (genetics), Seeds (metabolism), Sequence Alignment (MeSH), Trypsin Inhibitors (chemistry), Trypsin Inhibitors (genetics), Trypsin Inhibitors (metabolism).
MESH :
- chemical , chemistry : Receptors, Cell Surface, Trypsin Inhibitors.
- chemical , genetics : Receptors, Cell Surface, Trypsin Inhibitors.
- chemical , metabolism : Receptors, Cell Surface, Trypsin Inhibitors.
- genetics : Sapindaceae, Seeds.
- metabolism : Sapindaceae, Seeds.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Molecular Sequence Data, Sequence Alignment.

Abstract

Some proteins exhibit characteristics that suggest they have a primary, if not an exclusive role in nutrient reserve storage. The best studied examples are the storage proteins that accumulate specifically in developing seeds. Some of these protein demonstrate biological activities that could contribute to resistance to pest, pathogens or abiotic stresses. In this study we present the biochemical characterization and cloning of the major protein from seeds of T. esculenta (Talisin), a member of the Sapindaceae family. The N-terminal sequence of the protein isolated was used to produce a degenerated primer. This primer allowed the amplification of the Talisin cDNA by RTPCR from mRNA of the T. esculenta seeds protein. The sequence analysis of the cloned cDNA, demonstrated a 756 bp sequence encoding a peptide of 198 amino acids. The deduced peptide presented high similarity to a typical VSP, the 22-kDa protein in lychee (73 %) and 50.0 % identity to Theobroma bicolor reserve protein. Identities of 52.0 % and 44.0 % to trypsin inhibitors from Treobroma mammosum and Populus tremula respectively. In conclusion, we may suggest that Talisin could be a seed storage protein with affinity properties, i.e. interacts with carbohydrates and trypsin enzyme.

DOI: 10.2174/092986609789839287
PubMed: 20001918

Affiliations:

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Le document en format XML

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<author><name sortKey="Freire, Maria Das Gracas M" sort="Freire, Maria Das Gracas M" uniqKey="Freire M" first="Maria Das Graças M" last="Freire">Maria Das Graças M. Freire</name>
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<author><name sortKey="Oliveira, Marcos Vinicius" sort="Oliveira, Marcos Vinicius" uniqKey="Oliveira M" first="Marcos Vinïcius" last="Oliveira">Marcos Vinïcius Oliveira</name>
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<author><name sortKey="Filho, Goncalo Apolinario De Souza" sort="Filho, Goncalo Apolinario De Souza" uniqKey="Filho G" first="Gonçalo Apolinário De Souza" last="Filho">Gonçalo Apolinário De Souza Filho</name>
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<author><name sortKey="Oliveira, Marcos Vinicius" sort="Oliveira, Marcos Vinicius" uniqKey="Oliveira M" first="Marcos Vinïcius" last="Oliveira">Marcos Vinïcius Oliveira</name>
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<author><name sortKey="Filho, Goncalo Apolinario De Souza" sort="Filho, Goncalo Apolinario De Souza" uniqKey="Filho G" first="Gonçalo Apolinário De Souza" last="Filho">Gonçalo Apolinário De Souza Filho</name>
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<term>Molecular Sequence Data (MeSH)</term>
<term>Receptors, Cell Surface (chemistry)</term>
<term>Receptors, Cell Surface (genetics)</term>
<term>Receptors, Cell Surface (metabolism)</term>
<term>Sapindaceae (genetics)</term>
<term>Sapindaceae (metabolism)</term>
<term>Seeds (genetics)</term>
<term>Seeds (metabolism)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Trypsin Inhibitors (chemistry)</term>
<term>Trypsin Inhibitors (genetics)</term>
<term>Trypsin Inhibitors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Graines (génétique)</term>
<term>Graines (métabolisme)</term>
<term>Inhibiteurs trypsiques (composition chimique)</term>
<term>Inhibiteurs trypsiques (génétique)</term>
<term>Inhibiteurs trypsiques (métabolisme)</term>
<term>Récepteurs de surface cellulaire (composition chimique)</term>
<term>Récepteurs de surface cellulaire (génétique)</term>
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<term>Sapindaceae (génétique)</term>
<term>Sapindaceae (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
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<term>Trypsin Inhibitors</term>
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<term>Trypsin Inhibitors</term>
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<term>Trypsin Inhibitors</term>
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<term>Récepteurs de surface cellulaire</term>
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<term>Seeds</term>
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<term>Inhibiteurs trypsiques</term>
<term>Récepteurs de surface cellulaire</term>
<term>Sapindaceae</term>
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<term>Récepteurs de surface cellulaire</term>
<term>Sapindaceae</term>
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<term>Base Sequence</term>
<term>Cloning, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Sequence Alignment</term>
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<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
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<front><div type="abstract" xml:lang="en">Some proteins exhibit characteristics that suggest they have a primary, if not an exclusive role in nutrient reserve storage. The best studied examples are the storage proteins that accumulate specifically in developing seeds. Some of these protein demonstrate biological activities that could contribute to resistance to pest, pathogens or abiotic stresses. In this study we present the biochemical characterization and cloning of the major protein from seeds of T. esculenta (Talisin), a member of the Sapindaceae family. The N-terminal sequence of the protein isolated was used to produce a degenerated primer. This primer allowed the amplification of the Talisin cDNA by RTPCR from mRNA of the T. esculenta seeds protein. The sequence analysis of the cloned cDNA, demonstrated a 756 bp sequence encoding a peptide of 198 amino acids. The deduced peptide presented high similarity to a typical VSP, the 22-kDa protein in lychee (73 %) and 50.0 % identity to Theobroma bicolor reserve protein. Identities of 52.0 % and 44.0 % to trypsin inhibitors from Treobroma mammosum and Populus tremula respectively. In conclusion, we may suggest that Talisin could be a seed storage protein with affinity properties, i.e. interacts with carbohydrates and trypsin enzyme.</div>
</front>
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<Abstract><AbstractText>Some proteins exhibit characteristics that suggest they have a primary, if not an exclusive role in nutrient reserve storage. The best studied examples are the storage proteins that accumulate specifically in developing seeds. Some of these protein demonstrate biological activities that could contribute to resistance to pest, pathogens or abiotic stresses. In this study we present the biochemical characterization and cloning of the major protein from seeds of T. esculenta (Talisin), a member of the Sapindaceae family. The N-terminal sequence of the protein isolated was used to produce a degenerated primer. This primer allowed the amplification of the Talisin cDNA by RTPCR from mRNA of the T. esculenta seeds protein. The sequence analysis of the cloned cDNA, demonstrated a 756 bp sequence encoding a peptide of 198 amino acids. The deduced peptide presented high similarity to a typical VSP, the 22-kDa protein in lychee (73 %) and 50.0 % identity to Theobroma bicolor reserve protein. Identities of 52.0 % and 44.0 % to trypsin inhibitors from Treobroma mammosum and Populus tremula respectively. In conclusion, we may suggest that Talisin could be a seed storage protein with affinity properties, i.e. interacts with carbohydrates and trypsin enzyme.</AbstractText>
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Characterization of a saccharide-binding protein from Talisia esculenta seeds with trypsin inhibitory activity.

Characterization of a saccharide-binding protein from Talisia esculenta seeds with trypsin inhibitory activity.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki