Serum protein analysis by electrophoresis and by the Wolfson-Cohn chemical method; comparative study.

ONSIDERABLE TIME AND EFFORT has been devoted to the problem of fractionating serum protein simply, reliably, and rapidly, and at the same time in conformity with the free electrophoretic separation into albumin and a-, fi-, and 7-globulins. Much progress has been made, but discrepancies remain, especially in connection with aand -gIobulins. A few years ago Wolfson, Cohn, et at. (1) devised a relatively simple salting-out procedure for estimating the several serum-protein fractions, in a 1-mi. sample. The method involved four direct determinations: total protein, albumin, albumin plus a-globulin, and 7-globulin. All protein concentrations were determined by a modification of the Weichselbaum biuret method. Total globulin, a-globulin, and a-globulin were determined by calculation of differences between appropriate quantities. Popper et at. (2), using essentially this method, investigated serumprotein partition in a series of cases dominated by liver diseases. They found that the chemical (Wolfson-Cohn) albumin, total-globulin, and 7-globulin values, but not the aand $-globulin values, were well correlated with the corresponding electrophoretic values. This paper presents our appraisal of a slightly modified Wolfson-Cohn procedure, and an attempt at clarification of the observed discrepancies