FRACTIONATION ON DEAE-SEPHADEX OF NORMAL AND A-MYELOMA HUMAN SERA: I. ELECTROPHORETIC HETEROGENEITY OF γA GLOBULINS

Abstract

DEAE-Sephadex chromatography was employed to fractionate the γA globulins of normal and A-myeloma human sera. By immunoelectrophoresis, the normal γA globulins had mobilities ranging from that of γ1 to α2 globulins, whereas the myeloma γA globulins were of essentially uniform mobility. Most of the normal γA globulins were homogeneous with respect to sedimentation in a sucrose density gradient, indicating that their immunoelectrophoretic heterogeneity was due largely to differences in molecular charge rather than size.