Immunochemical studies are described in an unusual case of Waldenström's macroglobulinemia. Two monoclonal Igs (whole IgG1/kappa and IgG1/kappa half molecules) occurred in the serum in addition to the IgM monoclonal protein. Protein electrophoresis of the serum showed a monoclonal component in the gamma region, and the immunoelectrophoresis allowed detection of a monoclonal IgM/kappa and another abnormality represented by a double precipitin line in serum and urine, observed when antiserum anti IgG was used. The abnormal proteins were purified and further analyzed. The IgG-related proteins were whole four chains IgG monoclonal molecules, 1/2 IgG monoclonal molecules, composed of one heavy and one light chain, and residual polyclonal IgG. The half molecules were antigenically deficient with respect to normal IgG. The idiotypic analysis showed that the three monoclonal proteins shared idiotypic determinants. This patient had clinical and morphological findings of Waldenström's macroglobulinemia and, as observed in other cases, the formation of half molecules was not associated with a distinct clinical syndrome.

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The serum of a patient with a clinically and immunologically identified multiple myeloma of the IgE class was found to contain both IgE-albumin and IgG-albumin complexes. These complexes were partially purified and some of their properties studied by biochemical and immunoehemical methods. The IgG-albumin interaction was dissociated by 5.0 M guanidine hydrochloride, while the IgE-albumin interaction was dissociated upon reduction by mercaptoethanol, suggesting that the proteins were linked by intermolecular disulfide bonds. Complex formation between pathological or normal immunoglobulins with albumin have been reported for IgG, IgM and IgA but not for IgD or IgE. The present observation seems to be the first in which an IgE myeloma protein was involved.

UMPK 3 is a rare variant of the polymorphic enzyme of human red cells, uridine monophosphate kinase. This homozygote phenotype was detected among the Warao Indians of Venezuela. The UMPK 1 and UMPK 3 enzymes were partially purified following the method described by Tend et al. (1976). The biochemical and kinetic parameters of both variants were studied in crude hemolysates and in partially purified enzymes. A comparison was made with the results previously reported by Teng for UMPK 1 and UMPK 2, and it was concluded that UMPK 3 seems to resemble the other two allelic gene products in Km values for UMP, CMP, and ATP but differs from them in electrophoretic mobility, pH optimum, and thermal stability.