Source:http://linkedlifedata.com/resource/pubmed/id/11744631
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2001-12-17
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pubmed:abstractText |
Rate-zonal centrifugation of a reduced and alkylated respiratory mucin preparation identified a protein-rich fraction. This was subjected to trypsin treatment and one of the many liberated peptides was purified and its N-terminal sequence determined. The peptide was identical to a 14 amino acid sequence from the scavenger receptor cysteine-rich domain containing glycoprotein gp-340. A polyclonal antiserum, raised against the peptide, stained the serous cells in the submucosal glands of human tracheal tissue. The glycoprotein was purified from respiratory mucus by density-gradient centrifugation, gel chromatography, and anion exchange chromatography. The molecule exhibited a heterogeneous distribution of buoyant density (1.28-1.46 g/ml) that overlapped with the gel-forming mucins, was included on Sepharose CL-2B and was quite highly anionic. SDS-PAGE indicated a mass greater than 208 kDa and measurements performed across the molecular size distribution indicated an average M(r) of 5 x 10(5) with a range of M(r) from 2 x 10(5) to 1 x 10(6). Gel chromatography of respiratory mucus extracts ("associative" and "dissociative") indicated that this glycoprotein forms complexes that may involve the large gel-forming mucins MUC5AC and MUC5B. Rate zonal centrifugation suggested such complexes are more likely to involve MUC5B rather than MUC5AC mucins.
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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/MUC5B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Mucin-5B,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein 340
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0959-6658
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
969-77
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11744631-Amino Acid Sequence,
pubmed-meshheading:11744631-Humans,
pubmed-meshheading:11744631-Immunohistochemistry,
pubmed-meshheading:11744631-Macromolecular Substances,
pubmed-meshheading:11744631-Monosaccharides,
pubmed-meshheading:11744631-Mucin-5B,
pubmed-meshheading:11744631-Mucins,
pubmed-meshheading:11744631-Peptide Fragments,
pubmed-meshheading:11744631-Receptors, Immunologic,
pubmed-meshheading:11744631-Sequence Homology, Amino Acid,
pubmed-meshheading:11744631-Trachea
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pubmed:year |
2001
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pubmed:articleTitle |
Identification of a nonmucin glycoprotein (gp-340) from a purified respiratory mucin preparation: evidence for an association involving the MUC5B mucin.
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pubmed:affiliation |
Wellcome Trust Centre for Cell-Matrix Research, Division of Biochemistry, School of Biological Sciences, 2.205 Stopford Building, University of Manchester, Manchester, M13 9PT, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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