Nonionic surfactants in paper electrophoresis.

i-i E1IE HAVE BEEN a number of reports iii the literature regarding the use of surface active agents in zone electrophoretic studies of 1)100(1 serum proteins and hpoprotems. Ardr (1) found that cationic detergents formed, with serum protenis, complexes that migrated like $-lipoproteins, while aiiionic detergents formed complexes that clectrophoretically resembled -1ipoproteins. More recently, (irundy, J)obson, and Griffin (2) found that an anionic detergent, Lakeseal, caused an increased migration rate toward the anode of both and $-hpoprotenis, while a cationic detergent, beuzalkoniurn chloride, decrease(l migration toWar(l the anode and even caused the lipoprotems to move toWar(l the catho(le. They found that Tween 80, a nonionic surfactant, stopped lipoprotein migration completely. Grundv et a!. added the surfactants to the serum before electrophoresis and their results may not he comparable with those obtained where the materials were added to the buffer. ,J encks quoted by l)urrum (3) studied a number of nonionic surfactaiits. He concluded that these substances (limuhished the adsorption of alJ)unhin Oil l)ape1 hut obscured the protein-lipide relationship ut serum. Both I )owns et a!. (4) and Lloyd and Stewart (5), using Sterox SE and Lubiol \V, respectivel, found improved separations and increased numbers of protein or lipoprotein l)ahlds as a result of adding these compounds to the buffer.