Abstract
1. 1. A prolyl endopeptidase has been highly purified from eggs of the ascidian Halocynthia roretzi by ammonium sulfate fractionation and five chromatographic operations using DEAE-cellulose, DEAE-Sephacel, hydroxylapatite, Sephadex G-150 and Z-Gly-Pro-Leu-Gly-aminohexyl-Sephrose. 2. 2. The molecular weight and isoelectric point of the enzyme were estimated to 66,000 and 5.0, respectively. The pH optimum of the activity was 7.0–7.5. 3. 3. The enzyme was inactivated with diisopropylphosphorofluoridate, phenylmethylsulfonyl fluoride, Z-Gly-Pro-chloromethyl ketone and sulfhydryl-specific reagents; the susceptibility to these inhibitors was similar to that of the enzyme previously purified from spermatozoa of the same ascidian. 4. 4. The ranking of four prolinal-containing peptides in their inhibitory potencies to the egg enyzme was in good agreement with that to the sperm enzyme.
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