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PubMed1968

[Pyroglobulin].

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Humans↗
PubMed1986

IgD plasma cell leukemia associated with pyroglobulinemia and pyroglobulinuria.

A 70-yr-old man with multiple myeloma IgD developed a plasma cell leukemia producing a serum IgD monoclonal peak and lambda light chains in the urine. When the serum and the urine were heated at 56 degrees C for 30 min both monoclonal bands disappeared. The precipitate failed to redissolve on heating to 100 degrees C. Ion exchange chromatography with a linear gradient of phosphate buffer, pH 8, 0.020-0.300 mol/l and column electrofocusing showed that the serum pyroglobulin was eluted with buffer concentration between 0.040-0.125 mol/l and had an isoelectric point of 5.02, while the pyroglobulin of the urine was eluted with 0.020-0.033 mol/l and had a pI = 7.16. The serum and urine pyroglobulins had a total antigenic community with their correspondent purified proteins. The isolated lambda chains did not change when they were heated at 56 degrees C for 30 min, nevertheless, the heated purified IgD shows some changes in its isoelectric point, molecular mass and antigenicity. These changes in the purified IgD suggest that the pyroprecipitability could be due to conformational features.

Aged↗
PubMed1976

IgM pyroglobulinemia with erythrocytosis presenting as hyperviscosity syndrome. II. Biochemical properties and mechanisms of pyrogel formation.

An immunoglobulin M with kappa light chains (IgMK) pyroglobulin from a patient with hyperviscosity syndrome, erythrocytosis and coagulation defects has been studied for its immunochemical properties. At physiologic temperatures the purified macropyroglobulin showed a striking tendency to aggregate in the pentamer as well as in the monomer form. This property was also observed in its H chains. Aggregate formation of the pentamers may have contributed to the blood viscosity and coagulation defects. Formation of pyrogel at 56degreesC was observed with pentamers as well as monomers, but not with separated H or L chains. Amino acid analysis showed quantitative abnormalities of aspartic acid, glycine, cystine and leucine within the H chains. Solubility of the pyrogel in sodium dodecyl sulfate, the pyroglobulin's tendency to aggregate and the cystine deficit of H chains implicate conformational changes leading to hydrophobic bonding at 56degreesC in the formation of pyrogel.

Amino Acids↗
PubMed1988

IgE pyroglobulinemia in multiple myeloma.

A new case of IgE/K myeloma in a 38-year-old male is described. The clinical course, bone marrow picture and serum electrophoretic pattern were typical of multiple myeloma. Heating of the serum at 56 degrees C induced an irreversible gel formation or pyroglobulin that was isolated and proved to be identical to the IgE paraprotein, by biochemical and immunochemical methods. The thermoprecipitability was abolished by treatment with urea, sodium dodecyl sulphate and neutral salts and not inhibited by sugars, alcohols, 2-beta-mercaptoethanol and guanidine HCl. The association of an IgE myeloma protein with a pyroglobulin is a finding not previously reported in a myeloma of this class.

Adult↗