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Two‐dimensional electrophoretic analysis of immunoglobulin patterns in monoclonal gammopathies
Author(s) -
Goldfarb Marcia F.
Publication year - 1992
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150130191
Subject(s) - paraproteinemias , monoclonal , electrophoresis , antibody , monoclonal antibody , chemistry , immunology , biology , chromatography
Two‐dimensional (2‐D) electrophoresis was performed on 24 serum samples from patients diagnosed with monoclonal gammopathies. These samples had been shown to have a homogeneous immunoglobulin (M component) by zone electrophoresis and immunofixation. Using 2‐D electrophoresis, the nature of this aberrant protein was further analyzed. It has been presumed that the sharp, dark stained band identified by immunofixation was the production of a monoclonal immunoglobulin. The increased resolution afforded by 2‐D methodology reveals several different patterns. On 2‐D electrophoresis, a monoclonal antibody has a unique pattern. It consists of 3 to 6 strong, restricted heavy chain bands and a single distorted light chain spot. The 3–6 bands are microheterogeneity of the isoelectric point, attributed to posttranslational glycosylation and/or amidation/ deamidation. Analysis by 2‐D electrophoresis indicated only 5 samples with a true monoclonal pattern. All but 2 of the samples clearly had aberrant immunoglobulin, but interpretation of the pattern would suggest the protein is other than a fully synthesized monoclonal antibody. The samples showed the following: a monoclonal heavy chain pattern with multiple distorted light chain spots, only an aberrant light chain area, only an aberrant heavy chain, and only a polyclonal increase. Several IgG gammopathies had, in addition, concentrations of gamma heavy chain at a reduced size (34 kDa).