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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1988-11-10
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pubmed:abstractText |
The sequential removal of N-acetylneuraminic acid from rabbit serum transferrin has been followed by urea-polyacrylamide gel electrophoresis. The electrophoretic pattern is consistent with the presence of a single biantennary glycan chain. From the amino acid sequence of the carbohydrate-containing cyanogen bromide fragment we have shown that the glycan is attached to an asparaginyl side chain at a position equivalent to residue 491 in the sequence of human serum transferrin.
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pubmed:grant |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
238
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-42
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
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pubmed:year |
1988
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pubmed:articleTitle |
Evidence for a single glycan moiety in rabbit serum transferrin and location of the glycan within the polypeptide chain.
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pubmed:affiliation |
Division of Biochemistry, UMDS, Guy's Hospital, London, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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