Epitope mapping of snake venom phospholipases A2 with pseudexin monoclonal antibodies.
Identifieur interne : 002842 ( PubMed/Checkpoint ); précédent : 002841; suivant : 002843Epitope mapping of snake venom phospholipases A2 with pseudexin monoclonal antibodies.
Auteurs : B G Stiles [États-Unis] ; J L MiddlebrookSource :
- Journal of protein chemistry [ 0277-8033 ] ; 1991.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux, Calcium (métabolisme), Données de séquences moléculaires, Fixation compétitive, Phospholipases A (), Phospholipases A (immunologie), Phospholipases A2, Simulation numérique, Sites de fixation des anticorps, Souris, Souris de lignée BALB C, Structure moléculaire, Suidae, Séquence d'acides aminés, Test ELISA, Venins de serpent (), Venins des élapidés (), Venins des élapidés (immunologie), Épitopes (), Épitopes (analyse), Épitopes (immunologie).
- MESH :
- analyse : Épitopes.
- immunologie : Phospholipases A, Venins des élapidés, Épitopes.
- métabolisme : Calcium.
- Animaux, Anticorps monoclonaux, Données de séquences moléculaires, Fixation compétitive, Phospholipases A, Phospholipases A2, Simulation numérique, Sites de fixation des anticorps, Souris, Souris de lignée BALB C, Structure moléculaire, Suidae, Séquence d'acides aminés, Test ELISA, Venins de serpent, Venins des élapidés, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Antibody, Binding, Competitive, Calcium (metabolism), Computer Simulation, Elapid Venoms (chemistry), Elapid Venoms (immunology), Enzyme-Linked Immunosorbent Assay, Epitopes (analysis), Epitopes (chemistry), Epitopes (immunology), Mice, Mice, Inbred BALB C, Molecular Sequence Data, Molecular Structure, Phospholipases A (chemistry), Phospholipases A (immunology), Phospholipases A2, Snake Venoms (chemistry), Swine.
- MESH :
- chemical , analysis : Epitopes.
- chemical , chemistry : Elapid Venoms, Epitopes, Phospholipases A, Snake Venoms.
- chemical , immunology : Elapid Venoms, Epitopes, Phospholipases A.
- chemical , metabolism : Calcium.
- chemical : Antibodies, Monoclonal, Phospholipases A2.
- Amino Acid Sequence, Animals, Binding Sites, Antibody, Binding, Competitive, Computer Simulation, Enzyme-Linked Immunosorbent Assay, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Molecular Structure, Swine.
Abstract
Fifteen different monoclonal antibodies, developed against a pseudexin A, B, and C mixture, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin B were synthesized on alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies recognized linear epitopes of pseudexin A, pseudexin B, and also nonidentical sequences found in other phospholipases A2 (PLA2S) as determined by enzyme-linked immunosorbent assays. Three antibodies recognized a highly conserved site important in calcium binding and the interlocking of dimeric forms of PLA2. Antibodies neutralizing lethal or enzymatic effects of PLA2 did not recognize linear epitopes.
DOI: 10.1007/bf01024784
PubMed: 1718309
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:1718309Le document en format XML
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<term>Structure moléculaire</term>
<term>Suidae</term>
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<term>Test ELISA</term>
<term>Venins de serpent ()</term>
<term>Venins des élapidés ()</term>
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<term>Épitopes ()</term>
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<term>Épitopes (immunologie)</term>
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<term>Epitopes</term>
<term>Phospholipases A</term>
<term>Snake Venoms</term>
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<term>Binding Sites, Antibody</term>
<term>Binding, Competitive</term>
<term>Computer Simulation</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
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<term>Mice, Inbred BALB C</term>
<term>Molecular Sequence Data</term>
<term>Molecular Structure</term>
<term>Swine</term>
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<term>Phospholipases A</term>
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<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Fifteen different monoclonal antibodies, developed against a pseudexin A, B, and C mixture, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin B were synthesized on alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies recognized linear epitopes of pseudexin A, pseudexin B, and also nonidentical sequences found in other phospholipases A2 (PLA2S) as determined by enzyme-linked immunosorbent assays. Three antibodies recognized a highly conserved site important in calcium binding and the interlocking of dimeric forms of PLA2. Antibodies neutralizing lethal or enzymatic effects of PLA2 did not recognize linear epitopes.</div>
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<Abstract><AbstractText>Fifteen different monoclonal antibodies, developed against a pseudexin A, B, and C mixture, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin B were synthesized on alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies recognized linear epitopes of pseudexin A, pseudexin B, and also nonidentical sequences found in other phospholipases A2 (PLA2S) as determined by enzyme-linked immunosorbent assays. Three antibodies recognized a highly conserved site important in calcium binding and the interlocking of dimeric forms of PLA2. Antibodies neutralizing lethal or enzymatic effects of PLA2 did not recognize linear epitopes.</AbstractText>
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