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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1992-3-5
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Light Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin lambda-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0177-3593
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
372
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
835-43
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:1772596-Amino Acid Sequence,
pubmed-meshheading:1772596-Amyloid,
pubmed-meshheading:1772596-Amyloidosis,
pubmed-meshheading:1772596-Animals,
pubmed-meshheading:1772596-Cattle,
pubmed-meshheading:1772596-Horse Diseases,
pubmed-meshheading:1772596-Horses,
pubmed-meshheading:1772596-Humans,
pubmed-meshheading:1772596-Immune Sera,
pubmed-meshheading:1772596-Immunoglobulin Light Chains,
pubmed-meshheading:1772596-Immunoglobulin lambda-Chains,
pubmed-meshheading:1772596-Immunohistochemistry,
pubmed-meshheading:1772596-Molecular Sequence Data,
pubmed-meshheading:1772596-Molecular Weight,
pubmed-meshheading:1772596-Peptide Fragments,
pubmed-meshheading:1772596-Plasmacytoma,
pubmed-meshheading:1772596-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1772596-Skin,
pubmed-meshheading:1772596-Skin Diseases,
pubmed-meshheading:1772596-Swine
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Equine cutaneous amyloidosis derived from an immunoglobulin lambda-light chain. Immunohistochemical, immunochemical and chemical results.
|
| pubmed:affiliation |
Max-Planck-Institut für Biochemie, Martinsried bei München.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|