Chemical and Biological Properties of Fractions Derived from Hog Intrinsic Factor Concentrate by Disc Electrophoresis.

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Abstract
Summary HIFC was separated by polysaccharide disc electrophoresis into a distinct polysaccharide fraction (F-II), and 3 distinct protein fractions. Disc electrophoresis of the HIFC complexed with isotopically labelled vit B12 revealed that only one of these fractions (F-III), a protein devoid of stain-able polysaccharide, bound B12 avidly. When the losses due to processing are considered. F-III represents approximately 80% of the binding activity in the starting material. Following elution, F-III shows intrinsic factor activity by in vitro (guinea pig intestinal mu-cosal homogenate method) bioassay, and in vivo by Schilling's method in a patient with pernicious anemia, All other fractions were inert in vitro. Thus a protein moiety, free of polysaccharide, was responsible for both B12 binding and the specific enhancement of absorption. The sialic acid-containing major polysaccharide fraction (F-II) showed no significant B12 or in vitro activity.

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