Abstract
The isolated vascularly perfused rat intestine exhibits an obligatory need for a protein carrier in order to absorb zinc. Therefore this system is ideal for use as a model to identify the plasma carrier during zinc absorption. Affinity chromatography on Blue Sepharose CL-6B was employed to separate the major serum zinc-binding proteins in the portal effluent of the perfused intestine. It was found that 94% of newly absorbed 65Zn was transported in the portal serum-containing perfusate as an albumin-65Zn complex. The identity of albumin as the plasma carrier was confirmed by polyacrylamide-slab-gel electrophoresis. This evidence suggests that albumin is the plasma protein that is involved in removal of zinc from intestinal-mucosal cells and subsequent transport of the metal in portal blood to the liver.