Large‐scale purification of choline acetyltransferase and production of highly specific antisera

Publisher Website
Google Scholar
Abstract
Choline acetyltransferase (ChAT) was purified by immunoaffinity chromatography using a covalently immobilized monoclonal antibody. In a two‐step procedure, 10 kg porcine brain yielded 750 μg active enzyme of apparent homogeneity. This amount of ChAT was purified routinely. The purification factor was 18000 and the yield of activity 4.3%. The affinity resin was stable under the experimental conditions applied and was used many times. The highly purified enzyme was subsequently employed to obtain a specific anti‐ChAT antiserum of high titer.