Abstract
Ionic detergents were added to the human serum and to the egg white, and these protein systems were analyzed by the acrylamide gel electrophoresis. Detergents used were sodium dodecyl sulfate (SDS) and dodecyl trimethylammoniumbromide (DTAB). The zone of the complex AD2n (n=38), which is formed between the serum albumin and SDS, did not exist in the pattern of gel electrophoresis at pH 9.2. This is probably because of loosely bound SDS anions freed from AD2n during the gel electrophoresis to give ADm (m=11). The pre-albumin reacted with SDS and with DTAB to give several zones. In contrast to the serum albumin, the ovalbumin gave the zone of the complex ADn (n≥40), which is formed between ovalbumin and SDS. The effect of DTAB on ovalbumin is simply to precipitate it. The mobility of pre-albumin in egg white was not affected by either SDS or DTAB even at concentration as high as 150200mM. Reactions occurred quantitatively between some minor components and ionic detergents. Only lipoproteins in human serum were affected by nonionic detergent.
