MetalBindProtPlantV1, Main, Exploration, bibRecord, 000140

Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata.

Identifieur interne : 000140 ( Main/Exploration ); précédent : 000139; suivant : 000141

Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata.

Auteurs : Anamika Singh ; Purushotham Selvakumar ; Akhilesh Saraswat ; Prabhat P S. Tomar ; Manisha Mishra ; Pradhyumna K. Singh ; Ashwani K. Sharma [Inde]

Source :

Protein and peptide letters [ 1875-5305 ] ; 2015.

RBID : pubmed:26021386

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Hemagglutination Tests (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Murraya (chemistry), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Seed Storage Proteins (chemistry), Seed Storage Proteins (genetics), Seed Storage Proteins (metabolism), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH).
MESH :
- chemical , chemistry : Recombinant Proteins, Seed Storage Proteins.
- chemistry : Murraya.
- chemical , genetics : Recombinant Proteins, Seed Storage Proteins.
- chemical , metabolism : Recombinant Proteins, Seed Storage Proteins.
- Amino Acid Motifs, Amino Acid Sequence, Base Sequence, Hemagglutination Tests, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, Protein.

Abstract

A ~56 kDa protein having hemagglutination activity was purified and characterized from the Murraya paniculata seeds. The gel electrophoresis studies demonstrated that protein is primarily of two different subunits, molecular weight ~ 35 and 21 kDa held together by disulfide-linkages and predominantly by secondary forces. The cloning and sequence analysis revealed that the protein exhibited a substantial sequence identity to seed storage 11S globulin family proteins. The sequence analysis of Murraya paniculata globulin (MPG) demonstrated higher and lower molecular weight polypeptides to be acidic (α) and basic (β) respectively. The sequence analysis further showed that it possesses a characteristic bi-cupin motif and a putative metal binding pocket. CD analysis revealed that the MPG was a β/α protein with a slightly higher content of the former. Conformational changes in protein have been studied by fluorescence spectrometry by using various chemical treatments. The results demonstrated that MPG belongs to 11S globulin family and exhibit's hemagglutination activity, which implicates it to be possessing lectin-like property.

DOI: 10.2174/0929866522666150529161704
PubMed: 26021386

Affiliations:

Inde

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Le document en format XML

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<author><name sortKey="Singh, Anamika" sort="Singh, Anamika" uniqKey="Singh A" first="Anamika" last="Singh">Anamika Singh</name>
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<author><name sortKey="Selvakumar, Purushotham" sort="Selvakumar, Purushotham" uniqKey="Selvakumar P" first="Purushotham" last="Selvakumar">Purushotham Selvakumar</name>
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<author><name sortKey="Saraswat, Akhilesh" sort="Saraswat, Akhilesh" uniqKey="Saraswat A" first="Akhilesh" last="Saraswat">Akhilesh Saraswat</name>
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<author><name sortKey="Tomar, Prabhat P S" sort="Tomar, Prabhat P S" uniqKey="Tomar P" first="Prabhat P S" last="Tomar">Prabhat P S. Tomar</name>
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<author><name sortKey="Sharma, Ashwani K" sort="Sharma, Ashwani K" uniqKey="Sharma A" first="Ashwani K" last="Sharma">Ashwani K. Sharma</name>
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<author><name sortKey="Selvakumar, Purushotham" sort="Selvakumar, Purushotham" uniqKey="Selvakumar P" first="Purushotham" last="Selvakumar">Purushotham Selvakumar</name>
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<author><name sortKey="Singh, Pradhyumna K" sort="Singh, Pradhyumna K" uniqKey="Singh P" first="Pradhyumna K" last="Singh">Pradhyumna K. Singh</name>
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<author><name sortKey="Sharma, Ashwani K" sort="Sharma, Ashwani K" uniqKey="Sharma A" first="Ashwani K" last="Sharma">Ashwani K. Sharma</name>
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<term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Hemagglutination Tests (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Murraya (chemistry)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Seed Storage Proteins (chemistry)</term>
<term>Seed Storage Proteins (genetics)</term>
<term>Seed Storage Proteins (metabolism)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Analysis, Protein (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Analyse de séquence de protéine (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Murraya (composition chimique)</term>
<term>Protéines de stockage des graines (composition chimique)</term>
<term>Protéines de stockage des graines (génétique)</term>
<term>Protéines de stockage des graines (métabolisme)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Tests d'hémagglutination (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term>
<term>Seed Storage Proteins</term>
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<term>Protéines de stockage des graines</term>
<term>Protéines recombinantes</term>
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<term>Seed Storage Proteins</term>
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<term>Protéines recombinantes</term>
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<term>Seed Storage Proteins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de stockage des graines</term>
<term>Protéines recombinantes</term>
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<term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Hemagglutination Tests</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Sequence Alignment</term>
<term>Sequence Analysis, Protein</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<term>Analyse de séquence de protéine</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Motifs d'acides aminés</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
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<front><div type="abstract" xml:lang="en">A ~56 kDa protein having hemagglutination activity was purified and characterized from the Murraya paniculata seeds. The gel electrophoresis studies demonstrated that protein is primarily of two different subunits, molecular weight ~ 35 and 21 kDa held together by disulfide-linkages and predominantly by secondary forces. The cloning and sequence analysis revealed that the protein exhibited a substantial sequence identity to seed storage 11S globulin family proteins. The sequence analysis of Murraya paniculata globulin (MPG) demonstrated higher and lower molecular weight polypeptides to be acidic (α) and basic (β) respectively. The sequence analysis further showed that it possesses a characteristic bi-cupin motif and a putative metal binding pocket. CD analysis revealed that the MPG was a β/α protein with a slightly higher content of the former. Conformational changes in protein have been studied by fluorescence spectrometry by using various chemical treatments. The results demonstrated that MPG belongs to 11S globulin family and exhibit's hemagglutination activity, which implicates it to be possessing lectin-like property. </div>
</front>
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<Title>Protein and peptide letters</Title>
<ISOAbbreviation>Protein Pept Lett</ISOAbbreviation>
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<ArticleTitle>Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata.</ArticleTitle>
<Pagination><MedlinePgn>750-61</MedlinePgn>
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<Abstract><AbstractText>A ~56 kDa protein having hemagglutination activity was purified and characterized from the Murraya paniculata seeds. The gel electrophoresis studies demonstrated that protein is primarily of two different subunits, molecular weight ~ 35 and 21 kDa held together by disulfide-linkages and predominantly by secondary forces. The cloning and sequence analysis revealed that the protein exhibited a substantial sequence identity to seed storage 11S globulin family proteins. The sequence analysis of Murraya paniculata globulin (MPG) demonstrated higher and lower molecular weight polypeptides to be acidic (α) and basic (β) respectively. The sequence analysis further showed that it possesses a characteristic bi-cupin motif and a putative metal binding pocket. CD analysis revealed that the MPG was a β/α protein with a slightly higher content of the former. Conformational changes in protein have been studied by fluorescence spectrometry by using various chemical treatments. The results demonstrated that MPG belongs to 11S globulin family and exhibit's hemagglutination activity, which implicates it to be possessing lectin-like property. </AbstractText>
</Abstract>
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	Serveur d'exploration sur les protéines de liaison chez les plantes
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Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata.

Characterization and cloning of an 11S globulin with hemagglutination activity from Murraya paniculata.

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