The interaction of human serum protein fractions with the starch-iodine complex

Abstract

When starch-agar gel electrophoretic patterns are treated with iodine solution, decolorization in zones corresponding to the various protein fractions becomes more pronounced with time. This progressive loss of color cannot be ascribed entirely to the amylolytic activity since the starch-iodine reaction is influenced by serum proteins other than amylase. Increasing the starch concentration of iodine solution produces a relatively uniform rise in blue color intensity. However, this chromogenic response is greatly diminished by native human serum albumin or γ-globulin. The ability of these two fractions to dissipate starch-iodine color is lessened if the proteins are pre-iodinated. In the presence of fluoride, an amylase inhibitor, normal and pathologic sera are still capable of decolorizing starch-iodine solution to varying degrees. An interaction of serum proteins with available iodine would appear to account for this phenomenon.