rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1996-8-16
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pubmed:abstractText |
Matrix-assisted laser desorption mass spectrometry in combination with proteolytic protection assays has been used to identify the functional epitope on HIV-1 IIIB p26 recognized by a mAb. In this procedure, the intact protein is affinity bound to an immobilized mAb under physiologic conditions. A combination of proteolytic enzymatic cleavages was then performed to remove unprotected residues. Protected residues were identified by matrix-assisted laser desorption mass spectrometry based on their m.w. With this approach, an 11-residue sequence was identified as the most tightly affinity-bound fragment. in addition, two less tightly bound segments were observed. These latter two residues may contain elements of a discontinuous epitope or may be residues involved in a wider contact area. The combination of matrix-assisted laser desorption and proteolytic epitope footprinting has been applied to the determination of the epitope on a recombinant protein recognized by a mAb but should be equally applicable to the definition of an epitope on a native protein in its natural folded conformation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, gag,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gag Gene Products, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/gag protein p26, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/peptidyl-Lys metalloendopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-1767
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
157
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
198-206
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8683115-Amino Acid Sequence,
pubmed-meshheading:8683115-Antibodies, Monoclonal,
pubmed-meshheading:8683115-Antibody Affinity,
pubmed-meshheading:8683115-Epitope Mapping,
pubmed-meshheading:8683115-Epitopes,
pubmed-meshheading:8683115-Gene Products, gag,
pubmed-meshheading:8683115-HIV Antigens,
pubmed-meshheading:8683115-Humans,
pubmed-meshheading:8683115-Hydrolysis,
pubmed-meshheading:8683115-Metalloendopeptidases,
pubmed-meshheading:8683115-Molecular Sequence Data,
pubmed-meshheading:8683115-Recombinant Proteins,
pubmed-meshheading:8683115-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:8683115-gag Gene Products, Human Immunodeficiency Virus
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pubmed:year |
1996
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pubmed:articleTitle |
Epitope mapping by mass spectrometry: determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, National Institute of Environmental Health Science, Research Triangle Park, NC 27709, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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