Gamma-Globulin and Acquired Immunity to Human Malaria

tion than that resulting from the continuous system.Further, all y-globulin bands obtained by the discontinuous system were located closer to the albumin zone as noted previously 13 • Nevertheless, certain pathological y-globulins (lb, c, d) still migrated toward<;~ the cathode.Paper electrophoresis at pH 8•6 in citrate barbitur.ate buffer of the sera investigated demonstrated in each case a significant increase of the proteins which migrated with mobilities corresponding to those of the y-globulins.The increase over the normal value was 23-34 relative per cent.As judged by ultracentrifugal analysis the 78-globulins of the same sera varied between 30 and 40 per cent.The l9S-component appeared approximately normal in concentration.Abnormal plasma.proteins with sedimentation coefficients of 10 and 148, respectively, were observed in one case (le) only.The present starch-gel electrophoretic investigation on pathological y-globulins demonstrates that this procedure offers an advantage over paper electrophoresis in that certain abnormal y-globulins can be resolved into several bands.This resolution seems to indicate that these pathological y-globulins display a discontinuous spectrum with respect to apparent mobility in contrast to the continuous spectrum of the normal y-globulins.If the mobility of the 78-y-globulins may be related to the net charge of these molecules, then this observation can be interpreted to mean that certain pathological y-globulins are synthesized in such a way that they carry relatively unlike electrostatic net charges.This work was supported by