PubMed · 14152631
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
G CLOUGH, T G REAH. 1964-06-06. A "PROTEIN ERROR".. https://doi.org/10.1016/s0140-6736(64)91871-9
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Nonreducing two-dimensional gel electrophoresis (2-DE) is described for the study of immunoglobulin disorders with asynchronous production of single chains. Unlike classical reducing 2-DE, this method can distinguish between complex intact molecules and their free single chains (with different degrees of polymerization) and will thus be helpful for diagnosis of this type of disease. Examples are taken from canine patients, but the method may also be applied to both urine and serum specimens from other species. Nonreducing 2-DE thus represents a useful tool complementary to classical 2-DE, when further information about the appearance of free subunits or modifications of proteins are required, even in the presence of intact molecules.
Bence Jones protein in urine (immunoglobulin free-light-chains) is characteristic of light-chain multiple myeloma. We aimed to compare a quantitative immunoassay for serum free-light-chains with urine tests. Of 224 patients with light-chain myeloma tested at entry to clinical trials, all were correctly identified from serum samples. During monitoring of 82 patients, changes in serum and urine free-light-chains corresponded, but urine became negative for free-light-chains in 26 patients, whereas it remained abnormal in serum in 73 patients. Serum assays could replace Bence Jones protein urine tests for patients with light-chain multiple myeloma.
We report a case of mu-heavy chain disease. A 56-year-old woman presented with anemia and hemorrhagic diathesis. The serum of the patient was found to have free mu-heavy chain. The patient also had a kappa type-Bence Jones protein in serum and urine. Immunoelectrophoresis showed an abnormal precipitin line in the alpha 2-globulin region which reacted with antiserum to mu-chain but not with antiserum for light chains. The molecular weight of the monomer of the patient's mu-heavy chain protein was approximately 67,000 daltons less than that of the normal mu-heavy chain protein.