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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0185117,
umls-concept:C0332466,
umls-concept:C0597357,
umls-concept:C1511625,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1998793,
umls-concept:C2911684
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pubmed:issue |
4
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pubmed:dateCreated |
1992-12-14
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pubmed:abstractText |
Gene fusion has been used to produce the cytoplasmic domain of an endocytic receptor. DNA sequences coding for the 52 COOH-terminal amino acids of the mannose receptor from human macrophages, including the 41-amino acid cytoplasmic tail, were fused to the codons specifying the carbohydrate-recognition domain (CRD) of rat mannose-binding protein. The fusion protein was expressed in Escherichia coli and purified in one step on mannose-Sepharose, making use of the carbohydrate-binding activity of the CRD. The tail peptide was released from the fusion protein using endoproteinase Arg-C. This method provides an alternative to chemical synthesis for the production of midlength peptides.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectin,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/mannose binding protein A,
http://linkedlifedata.com/resource/pubmed/chemical/mannose receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1046-5928
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
308-12
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1422224-Amino Acid Sequence,
pubmed-meshheading:1422224-Animals,
pubmed-meshheading:1422224-Base Sequence,
pubmed-meshheading:1422224-Carrier Proteins,
pubmed-meshheading:1422224-Chromatography, Affinity,
pubmed-meshheading:1422224-Endocytosis,
pubmed-meshheading:1422224-Endopeptidases,
pubmed-meshheading:1422224-Humans,
pubmed-meshheading:1422224-Lectins, C-Type,
pubmed-meshheading:1422224-Macrophages,
pubmed-meshheading:1422224-Mannose,
pubmed-meshheading:1422224-Mannose-Binding Lectin,
pubmed-meshheading:1422224-Mannose-Binding Lectins,
pubmed-meshheading:1422224-Molecular Sequence Data,
pubmed-meshheading:1422224-Peptide Fragments,
pubmed-meshheading:1422224-Rats,
pubmed-meshheading:1422224-Receptors, Cell Surface,
pubmed-meshheading:1422224-Receptors, Immunologic,
pubmed-meshheading:1422224-Recombinant Fusion Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Expression and purification of the cytoplasmic tail of an endocytic receptor by fusion to a carbohydrate-recognition domain.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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