rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1993-9-14
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pubmed:abstractText |
CAMPATH-1 antibodies recognize a unique molecule on human lymphocytes and are unusually efficient at causing cell lysis with homologous complement. They have been successfully used for lymphocyte depletion in vivo in a variety of diseases. We find that the antigen is a very small glycosylphosphatidylinositol (GPI)-anchored glycoprotein with a mature peptide comprising only 12 amino acids. It can be separated into two distinct antigenic fractions which differ in their susceptibility to phosphatidylinositol-specific phospholipase C. There is one N-linked glycosylation site, but no evidence for O-glycosylation despite the presence of several serine and threonine residues. The antibodies were found to bind, albeit with a generally reduced affinity, to a proteolytic fragment containing the C-terminal tripeptide and the GPI anchor. We postulate that one of the reasons why the CAMPATH-1 antibodies are so good for cell lysis is because they bind to an epitope which is likely to be very close to the lipid bilayer.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7688956-1327504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7688956-1352921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7688956-1397606,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7688956-81133
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CD52 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Complement System Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
293 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
633-40
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:7688956-Antibodies,
pubmed-meshheading:7688956-Complement System Proteins,
pubmed-meshheading:7688956-Glycoproteins,
pubmed-meshheading:7688956-Protein Conformation,
pubmed-meshheading:7688956-Epitopes,
pubmed-meshheading:7688956-Amino Acid Sequence,
pubmed-meshheading:7688956-Molecular Sequence Data,
pubmed-meshheading:7688956-Hydrolysis,
pubmed-meshheading:7688956-Antigens, Neoplasm,
pubmed-meshheading:7688956-Pronase,
pubmed-meshheading:7688956-Sequence Homology, Amino Acid,
pubmed-meshheading:7688956-Binding Sites, Antibody,
pubmed-meshheading:7688956-Antigens, CD
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