Abstract
Two vitamin B12 binding components were separated from the hog intrinsic concentrate WES 942 by recycling gel filtration and examined for enhancing effect on the uptake of B12 by tissue homogenates. Only the minor component, B, which according to an earlier study possessed intrinsic factor identity, enhanced the uptake of B12 by guinea pig intestinal mucosa homogenate. Only the major B12 binding component, A, which had earlier been found to lack intrinsic factor identity, enhanced the uptake of B12 by rat-liver homogenate.