Electrophoretic properties of ovomucoid

Abstract

The nature of the electrophoretic heterogeneity of ovomucoid was investigated. Optimum resolution of the fractions on starch-gel electrophoresis occurred over a narrow range of pH and ionic strength. The pattern was not altered in the presence of 8 [image]-urea but the bands were sharper. Ovomucoid-trypsin complex is stable at pH 4.6 but dissociated in 6 [image]-urea. The 2 major fractions of ovomucoid were eluted from the gels. One of these was virutally free of sialic acid and the other, which contained 0.4 mole of sialic acid/mole of protein, split into 2 components on electrophoresis after neuraminidase treatment. It was concluded that these 2 components, and likewise the 2 major fractions of ovomucoid, differ by a unit charge/mol. Differences in sialic acid content account for only part of the electrophoretic heterogeneity of ovomucoid.