A Starch Gel Immunoelectrophoretic Analysis of Human γ-Globulin demonstrating the Inter- and Intra-Specific Variation of Organisms

Abstract

AN age-dependent, phenotypic variation in the antigenic composition of human γ₂-globulin has been reported^1–3. Chicken antisera to preparations rich in γ-globulin (for example, FrII) were used to examine human sera by the starch gel immuno-electrophoretic method of Poulik⁴as modified by Goodman^3,5. Certain of these antisera detected in many instances more than one component in that portion of the γ-globulin which moves backward from the origin in starch gel electrophoresis, that is, in the γ₂fraction of serum. Recently, as the point of departure for the present work, non-human primate sera were also examined by some of the antisera. It was reasoned that, since the evolutionary continuum leads from the intra- to the inter-specific variation of organisms, the serum antigenic specificities which differ between human beings would fail to have derivative counterparts in the sera of the non-human primates. A considerable body of data illustrating the applications of this reasoning has now been gathered, and several examples of the data are presented in Figs. 1 and 2.