George M. Bernier

GAMMA GLOBULIN ANTIGENIC TYPES DEFINED BY HEAVY CHAIN DETERMINANTS.

Two populations of immunologically distinguishable 7S gamma globulins in normal human serum and two corresponding antigenic types of myeloma 7S gamma globulins have been detected with rabbit antiserums to proteins associated with pathological conditions, the differences being related to the H-chains of 7S gamma globulin. No relationship exists with type I and type II antigenic classification, determined by L-chains. Human serums with various hereditary gamma globulin (Gm) specificities contain both types of 7S gamma globulin.

Polymerism, polymorphism, and impurities in Bence-Jones proteins

Abstract The heterogeneity exhibited by Bence-Jones proteins in starch gel electrophoresis was found to be due to contamination with other proteins of diverse origins and to the presence of polymeric and polymorphic forms of Bence-Jones proteins. Isolation of purified major components of four Bence-Jones proteins was achieved by ion-exchange chromatography and gel filtration. Minor components were isolated by these means and were found to account for the three types of heterogeneity described. The Characteristic of dissolution at high temperatures, long considered a specific property of Bence-Jones proteins, was found to be shared by other proteins when the temperature range was extended above 100°.

Microglobulinaemia in renal failure.

IMPAIRMENT of renal function is associated with body retention of certain simple organic compounds such as urea, creatinine and uric acid. We describe here the occurrence of markedly increased concentrations of a low molecular weight protein in the sera of patients with renal failure. Neither the mechanism nor the physiological consequences of this abnormality are evident, but a defect in the renal catabolism of the protein may be responsible for this selective hyperproteinaemia.

Crystallocryoglobulinemia Resulting from Human Monoclonal Antibodies to Albumin

Two patients had a previously unrecognized form of crystallocryoglobulinemia. Their clinical presentations were similar, consisting of necrotizing vasculitis and purpura involving the legs. Analysis of each cryoglobulin complex showed that two components, albumin and a monoclonal IgG-lambda, were present, and both components were needed in a fixed ratio for precipitation. In addition, cryoprecipitation occurred in serum, but not plasma, due to citrate inhibition of complex formation. Our findings suggest that the monoclonal IgGs have the properties of antibodies directed specifically against a calcium-dependent antigenic site on human albumin, and that the resultant IgG-lambda-albumin immune complexes crystallized in the cold.

The source of the apparent carbohydrate content of Bence-Jones proteins

Abstract Bence-Jones proteins prepared by repeated ammonium sulfate precipitation appear to contain variable amounts of carbohydrate. This has been shown to be due to contamination by other carbohydrate-containing substances. Fractions with high hexose contents were isolated from a Bence-Jones protein preparation, and similar materials appeared to be present in all the carbohydrate-containing proteins that were tested.

Plasma Cell Leukemia with Excretion of Half-Molecules of Immunoglobulin A (α1 λ1)

: A patient with plasma cell leukemia and myelofibrosis excreted free immunoglobulin light chains and an abnormal monoclonal immunoglobulin (Ig) A in her urine. The IgA that was present in serum and urine had a sedimentation coefficient of 4.0 S. The molecule was comprised of both heavy and light chains but was antigenically deficient compared to normal IgA. As excreted in the urine, the protein appeared to be a half-molecule of IgA, with a partial deletion in the heavy chain, probably involving part or all of the C-terminal domain.