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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1992-11-6
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pubmed:abstractText |
We studied several monoclonal antibodies (mAbs) raised against the 100 kD Ras GTPase activating protein (p100-GAP), which was purified from human placenta. These antibodies recognized p120-GAP and p100-GAP in native and in denatured forms. The most reactive, GP15 and GP200, both recognized distinct epitopes and did not neutralize GTPase stimulatory activity. These two mAbs were selected for a two-site enzyme immunoassay, using covalent conjugates of the antibodies coupled to the tetrameric form of acetylcholinesterase as tracer. This assay was used to quantify Ras-GAP in both normal and tumor tissues and cell extracts.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
B
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0733-222X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1151-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1368795-Animals,
pubmed-meshheading:1368795-Antibodies, Monoclonal,
pubmed-meshheading:1368795-Cell Line,
pubmed-meshheading:1368795-Choriocarcinoma,
pubmed-meshheading:1368795-GTPase-Activating Proteins,
pubmed-meshheading:1368795-Genes, ras,
pubmed-meshheading:1368795-Humans,
pubmed-meshheading:1368795-Immunoenzyme Techniques,
pubmed-meshheading:1368795-Mice,
pubmed-meshheading:1368795-Placental Extracts,
pubmed-meshheading:1368795-Proteins,
pubmed-meshheading:1368795-ras GTPase-Activating Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Non-neutralizing monoclonal antibodies against Ras GTPase-activating protein: production, characterization and use in an enzyme immunometric assay.
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pubmed:affiliation |
INSERM U. 245, Hôpital Saint-Antoine, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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