• 1 July 1971
    • journal article
    • Vol. 9  (1) , 11-20
Abstract
When examined by immunoelectrophoresis and double-gel diffusion, gastric acid-stable esterase (VI A) and human intrinsic factor (IF) behaved as different substances. The VI A migrated in agar-gel electrophoresis mainly as a β2/β1-globulin and IF as β1/α2-globulin. Both showed overlapping migration and diffusion near the starting point. On DEAE-chromatography IF was eluted together with VI A at 0·05–0·075 M, pH 7·0. In gel filtration experiments with Sephadex G 100 and G 200, the IF from in vivo neutralized gastric juice (NGJ) and from gastric mucosa (GM) was eluted in a definite range according to its molecular weight of 60,000. No IF was found in acid gastric juice (AGJ).