| pubmed-article:2412547 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C0017911 | lld:lifeskim |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:2412547 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:2412547 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2412547 | pubmed:dateCreated | 1985-9-27 | lld:pubmed |
| pubmed-article:2412547 | pubmed:abstractText | Tyrosine-glycogen obtained from retina proteoglycogen by exhaustive proteolytic digestion was radiolabelled with 125I. The 125I-labelled tyrosine-glycogen was degraded by amylolytic digestion to a very small radioactive product, which was identified as iodotyrosine by h.p.l.c. The amylolytic mixture used released glucose and maltose that were alpha-linked to the phenolic hydroxy group of p-nitrophenol. No free iodotyrosine was found before or after the intact [125I]iodotyrosine-glycogen was subjected to two cycles of the Edman degradation procedure. The linkage between protein and glycogen was alkali-stable. Therefore it is concluded that the protein-bound glycogen was O-glycosidically linked to the phenolic hydroxy group of tyrosine. The amino acid has not been heretofore found to be involved in the linkage of carbohydrates to proteins. | lld:pubmed |
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| pubmed-article:2412547 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2412547 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2412547 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2412547 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2412547 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2412547 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2412547 | pubmed:author | pubmed-author:CurtinoJ AJA | lld:pubmed |
| pubmed-article:2412547 | pubmed:author | pubmed-author:AlyM SMS | lld:pubmed |
| pubmed-article:2412547 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2412547 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2412547 | pubmed:volume | 229 | lld:pubmed |
| pubmed-article:2412547 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2412547 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2412547 | pubmed:pagination | 269-72 | lld:pubmed |
| pubmed-article:2412547 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2412547 | pubmed:meshHeading | pubmed-meshheading:2412547-... | lld:pubmed |
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| pubmed-article:2412547 | pubmed:meshHeading | pubmed-meshheading:2412547-... | lld:pubmed |
| pubmed-article:2412547 | pubmed:meshHeading | pubmed-meshheading:2412547-... | lld:pubmed |
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| pubmed-article:2412547 | pubmed:meshHeading | pubmed-meshheading:2412547-... | lld:pubmed |
| pubmed-article:2412547 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2412547 | pubmed:articleTitle | Protein-bound glycogen is linked to tyrosine residues. | lld:pubmed |
| pubmed-article:2412547 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2412547 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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