PHYSICOCHEMICAL CHARACTERIZATION OF MOUSE MYELOMA PROTEINS: DEMONSTRATION OF HETEROGENEITY FOR EACH MYELOMA GLOBULIN

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Abstract
Physicochemical characterization of 20 mouse myeloma proteins revealed the individuality of each myeloma protein. When the myeloma proteins are considered collectively, a wide range of individual properties were represented, including electrophoretic mobilities varying from the gamma to alpha region, hexose content from 1 to 4% and ultracentrifugal components from 6.5S to 13S. The 20 myeloma proteins could be divided into groups, the gamma type and the B2A myeloma globulins, on the basis of physicochemical and immunoelectrophoretic studies. Two types of heterogeneity were observed. Polymer formation was responsible for the 9S, US and/or 13S components seen on ultracentrifugation of the [beta]2A myeloma proteins. Starch gel electrophoresis revealed relatively widely separated myeloma protein components in these sera, presumably due to the retardation effect of the gel on the electrophoretic migration of the larger polymers. Starch gel electrophoresis revealed a different type of heterogeneity (electrophoretic heterogeneity) for the 2 gamma-type myeloma proteins. These contained 5 or more components with closely related but not identical electrophoretic properties. The physicochemical characteristics of the gamma-type and [beta]-type myeloma proteins in the mouse indicated the close similarity of these proteins to the gamma and [beta]2a myeloma proteins in man.