| pubmed-article:1772596 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C0019944 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C0021027 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C0268397 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C1441616 | lld:lifeskim |
| pubmed-article:1772596 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:1772596 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:1772596 | pubmed:dateCreated | 1992-3-5 | lld:pubmed |
| pubmed-article:1772596 | pubmed:abstractText | Amyloid deposits from equine cutaneous nodular amyloidosis associated with extramedullary plasmacytoma were classified immunohistochemically as equine immunoglobulin lambda-light chain-derived and designated eA lambda (HIP). For chemical identification, the amyloid fibril proteins were separated on Sephadex G-100 in 6M guanidine.HCl. Polypeptides of predominantly 24 kDa and 50 kDa were found by polyacrylamide gel electrophoresis. They have preponderance of immunoglobulin lambda-antigenic determinants as detected by immunodiffusion and immunoblotting. Since the N-terminus of the major proteins was blocked, peptides were generated with trypsin and endoproteinase Asp-N and then isolated using reversed-phase high-performance liquid chromatography. Automatic amino-acid sequence determination of seven peptides showed novel sequences. Data bank comparison indicated that these peptides were derived from a monoclonal immunoglobulin lambda-light and a gamma-heavy chain. The light chain was considered to be the leading amyloidogenic polypeptide, since it was the predominant component in a virtually pure amyloid fibril preparation. Thus, immunoglobulin lambda-light chain-derived amyloidosis, so far established only in man and cat, has now also been identified in the horse. | lld:pubmed |
| pubmed-article:1772596 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1772596 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1772596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1772596 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1772596 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1772596 | pubmed:issn | 0177-3593 | lld:pubmed |
| pubmed-article:1772596 | pubmed:author | pubmed-author:MannKK | lld:pubmed |
| pubmed-article:1772596 | pubmed:author | pubmed-author:LinkeR PRP | lld:pubmed |
| pubmed-article:1772596 | pubmed:author | pubmed-author:GeiselOO | lld:pubmed |
| pubmed-article:1772596 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1772596 | pubmed:volume | 372 | lld:pubmed |
| pubmed-article:1772596 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1772596 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1772596 | pubmed:pagination | 835-43 | lld:pubmed |
| pubmed-article:1772596 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
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| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
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| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:meshHeading | pubmed-meshheading:1772596-... | lld:pubmed |
| pubmed-article:1772596 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1772596 | pubmed:articleTitle | Equine cutaneous amyloidosis derived from an immunoglobulin lambda-light chain. Immunohistochemical, immunochemical and chemical results. | lld:pubmed |
| pubmed-article:1772596 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Martinsried bei München. | lld:pubmed |
| pubmed-article:1772596 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1772596 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1772596 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
