The Iron-Binding Glycoprotein of Human Gastric Juice. II. Nature of the Interaction of the Glycoprotein with Iron

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Abstract
The nature of the interaction between a gastric iron-binding glycoprotein and iron has been studied. These experiments showed that much of the iron could be separated from the glycoprotein by the physical methods of filtration and centrifugation. Magnetic susceptibility measurements were compatible with the presence of polymerized ferric hydroxide in the iron glycoprotein complex and such iron particles were subsequently visualized by electron microscopy. Spectroscopic studies failed to show any absorption peaks or shifts which could be attributed to the chemical interaction of iron and some group on the glycoprotein. Hence it was concluded that the glycoprotein exerted its influence by maintaining colloidal iron particles in suspension. Experiments in rats testing the absorption of iron from the iron glycoprotein complex showed that the iron was appreciably better absorbed from the complex than from an acid solution of ferric chloride. Furthermore the absorption of iron from the iron glycoprotein complex was of the same order as absorption from neutral solutions of iron-containing ascorbate. The possible role of this gastric glycoprotein in iron absorption is discussed.

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