Abstract
1. 1. Trypsin from digestive gland of the shrimp Penaeus japonicus has been purified 26-fold by gel filtration affinity chromatography and ion exchange chromatography. 2. 2. Optimum pH was found to be around 8–8.3 and the enzyme was stable for several days at pH 8. The enzyme activity was inhibited by standard trypsin inhibitors but not enhanced by CaCl 2. 3. 3. After electrophoresis, six fractions hydrolyse the synthetic substrate BANA. All these fractions have the same mol. wt of about 25,000 as determined by SDS electrophoresis. 4. 4. Antiserum against shrimp trypsin was prepared. Trypsin activity during the intermolt cycle is correlated with enzyme quantity as shown by electroimmunoassay.
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