Abstract
1. 1. Ostrich aminopeptidase was purified by salt fractionation, Sephadex G-200 and DEAE-Toyopcarl 650M chromatography of a pH 6.9 duodenal extract. 2. 2. The final preparation was homogeneous when subjected to gradient gel electrophoresis with a M r of 290,000. 3. 3. The effects of pH, temperature and metal ions on aminopeptidase activity were examined. 4. 4. Kinetic parameters ( K m, k cat and k cat/ K m) for two substrates (APNA and LPNA) were determined.
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