I. Genetic studies of mouse serum protein types. II. Molecular hybridization of sheep hemoglobins

NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document. Investigations were conducted to detect serum protein variant systems in mice and to define their genetic control. Three systems were detected. A pair of codominant alleles at a locus in the second linkage group controls electrophoretically different transferrin types. An electrophoretic difference among inbred lines in the presence or absence of a prealbumin is controlled by a single autosomal locus without dominance. A serologically detected system is controlled by a single locus closely linked or identical to the H-2 locus in the ninth linkage group. The variant component seems to be an [alpha]-globulin of high molecular weight. The principal difference between serum types is quantitative; qualitative differences are not excluded. The serum component is not detectably related serologically to H-2 erythrocyte antigens. The effects of development, pregnancy and stress upon these serum components were studied. Using these three serum variants as markers, the sera of homologous radiation chimeras were examined for donor type proteins. These occasionally appear transitorily, but long-term survivors having entirely donor erythrocytes have only host type serum proteins. Molecular hybridizations were performed with the two known sheep hemoglobin variants. Radioactive and ferriheme labels showed some exchange of subunits between variant types, but less than expected. Incomplete exchange is apparently due to inadequate asymmetric dissociation or to partial incompatibilities between both subunits of the two hemoglobins. The electrophoretic difference between the two types resides mainly, if not entirely, in one of the subunits