Linked Life Data

2518742

Source:http://linkedlifedata.com/resource/pubmed/id/2518742

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1991-6-6
pubmed:abstractText
The monoclonality of myeloma proteins is usually demonstrated by their electrophoretic homogeneity and their reactivity with monovalent antisera directed against isotypic determinants of a single heavy chain and a single type of light chain. The absence of precipitation with anti-sera to immunoglobulin kappa and Lambda light chains is a constant character of heavy Chain Disease Proteins (HCDP). However, homogeneous M-components present in the sera of some patients and reacting only with anti-heavy-chain antisera were identified as IgA and IgD myeloma proteins bearing unreactive Lambda chains. In this study, the electrophoretic pattern of a patient serum showed a paraprotein with heterogeneous electrophoretic mobility and precipitation reaction limited to anti-IgD antiserum. The failure to react with anti-light chain antisera was observed by immuno-electrophoresis, immunofixation and rocket-immunoselection. Further analysis by crossed-immunoelectrophoresis revealed that IgD paraprotein contained two separate populations of molecules, one of them being retained when anti-Kappa and Lambda light chains anti-bodies were incorporated in the first dimension gel. It soon became obvious that the observed pattern was generated by enzymatic cleavage of native IgD myeloma protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-2460
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-40
pubmed:dateRevised
2007-3-9
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Spontaneous enzymatic cleavage of IgD myeloma protein giving a pattern of delta heavy chain disease.
pubmed:publicationType
Journal Article