Human Gastric Antigens I. The Purification and Preliminary Characterization of the Antigenic, Acid‐Stable Carboxyl Esterase VI A*
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TL;DR
Preliminary characterization studies showed that the gastric antigen was purified by gel filtration and anion exchange chromatography from gastric juice is a heat‐ and acid‐stable antigen with the enzymatic activity of a non‐specific carboxyl esterase with a pH optimum between pH 6.4 and 6.8.
Abstract
Abstract. A gastric antigen with enzymatic activity (VI A) was purified by gel filtration and anion exchange chromatography from gastric juice. Rabbits were immunized with the pure antigen and produced highly specific precipitating antibodies. The specific antisera were subsequently used as immunoadsorbents for a one‐step purification procedure. The immunoadsorption technique yielded a pure antigen fraction. When gastric mucosa or gastric juice neutralized in vivo were used as starting materials instead of acid gastric juice, two serum proteins, IgG and albumin, were eluted with the antigen. During gel filtration two different molecular forms of the antigen were observed. The antigen obtained for gastric juice had a molecular weight of 140000, whereas the antigen from gastric mucosa had a molecular weight of approximately 70000. The antigen obtained by different purification procedures showed immunological identity. Preliminary characterization studies showed that the antigen is a heat‐ and acid‐stable antigen with the enzymatic activity of a non‐specific carboxyl esterase with a pH optimum between pH 6.4 and 6.8.