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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
1991-8-7
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pubmed:abstractText |
To determine the epitopic structure for an anti-GalNAc alpha-Ser(Thr) (anti-Tn) monoclonal antibody, MLS 128, asialo-ovine submaxillary mucin was digested with various proteases, and the digests were fractionated by immunoaffinity column chromatography and high performance liquid chromatography. From the tryptic digest, a glycopeptide, GP-I, and five other glycopeptides, GP-1-5, were obtained as bound and unbound fractions, respectively, of the immunoaffinity column. By solid phase radioimmunoassaying, it was found that GP-I was strongly immunoreactive, whereas GP-1-5 were poorly immunoreactive. On treatment with V8 protease, GP-I was converted to two glycopeptides, one with poor reactivity and the other with intermediate reactivity. From the thermolysin digest, the smallest fragment, GP-II, was isolated, which was as strongly immunoreactive as GP-I. GP-II corresponded to a part of GP-I, its sequence being Leu-Ser*-Glu-Ser*-Thr*-Thr*-Gln-Leu-Pro-Gly, where asterisks denote amino acids to which an alpha-GalNAc residue is attached. Other anti-Tn monoclonal antibodies, NCC-LU-35 and CA 3239, showed essentially the same reactivity to these glycopeptides as MLS 128 did. The glycopeptides (GP-1-5), which exhibited poor immunoreactivity, contained various GalNAc-containing structures, such as GalNAc-Ser, GalNAc-Thr, GalNAc-Ser-(GalNAc)-Ser, and GalNAc-Thr-(GalNAc)-Thr. These results indicate that a glycopeptide including a cluster structure, Ser*-Thr*-Thr*, is an essential part of the epitope recognized by anti-Tn antibodies.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Asialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/Thermolysin,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12402-5
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pubmed:dateRevised |
2007-12-1
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pubmed:meshHeading |
pubmed-meshheading:1712019-Amino Acid Sequence,
pubmed-meshheading:1712019-Animals,
pubmed-meshheading:1712019-Antibodies, Monoclonal,
pubmed-meshheading:1712019-Asialoglycoproteins,
pubmed-meshheading:1712019-Carbohydrates,
pubmed-meshheading:1712019-Chromatography, Affinity,
pubmed-meshheading:1712019-Chromatography, High Pressure Liquid,
pubmed-meshheading:1712019-Epitopes,
pubmed-meshheading:1712019-Glycopeptides,
pubmed-meshheading:1712019-Molecular Sequence Data,
pubmed-meshheading:1712019-Mucins,
pubmed-meshheading:1712019-Protein Conformation,
pubmed-meshheading:1712019-Radioimmunoassay,
pubmed-meshheading:1712019-Sheep,
pubmed-meshheading:1712019-Submandibular Gland,
pubmed-meshheading:1712019-Thermolysin,
pubmed-meshheading:1712019-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
Elucidation of an essential structure recognized by an anti-GalNAc alpha-Ser(Thr) monoclonal antibody (MLS 128).
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pubmed:affiliation |
Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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