Präparative Elektrophorese von Elastase. Einfluß von Metallionen auf das Enzym

Publisher Website
Google Scholar
Abstract
Partially purified elastase was further purified by continuous paper electrophoresis. The sharpest separation of enzyme from residual proteins was obtained in 1.5% pyridine containing 0,015 M calcium acetate. The best runs gave an 80% yield, specific activity 160 elastase units/mg. In the absence of Ca2, the separation was insignificant and the yield poor. To prepare elastase free from trypsin, the contaminant trypsin was largely inactivated at pH 8.8 and then completely inactivated with Soya bean trypsin inactivator prior to electrophoresis. This also caused a small but tolerable decrease in the elastase activity. The finally purified enzyme was free from trypsin, chymotrypsin, amino-peptidase and carboxypeptidase. The purification was 214 fold in relation to the starting material, pancreatin. The yield of freeze dried enzyme was 6.2%. Ca2 ions stabilize the enzyme protein of elastase.