Preparation of amine oxidase from bovine serum by affinity chromatography on aminoheyxyl-Sepharose.

Amine oxidase was purified from bovine serum by affinity chromatography on aminohexyl substituted Sepharose. The enzyme was adsorbed on the chromatographic support in a suspension of aminohexyl Sepharose in diluted serum. After thorough washing with buffer, the gel was packed in a column and the enzyme eluted with 10 mM octylamine. Using this procedure it was possible to obtain apparently homogeneous amine oxidase in a single-step procedure. The specific enzyme activity was 0.14 mumoles benzaldehyde formed per minute at 25 degrees C per mg enzyme protein. Based on the activity of amine oxidase in serum, the yield of enzyme was 64%.