Studies on Pituitary Catkepsin D with Artificial Substrates

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Abstract
A proteolytic enzyme acting at acidic pH has been partially purified from bovine anterior pituitary. It was found to hydrolyze the artificial substrate, Z-Pro-Phe-His-Leu-Leu-Val- Tyr-Ser-ß-naphthylamide at the Phe-His and the Leu-Leu bonds. This hydrolysis serves as basis of a sensitive fluorimetrie assay. The enzyme is similar to cathepsin D. The pentapeptides Z-Pro- Phe-His-Leu-Leu-β-naphthylamide and Z-Leu-Leu-Val-Tyr-Serß- naphthylamide were also attacked, but at a much slower rate. Smaller substrates were not hydrolyzed. The results indicate that the enzyme preferentially hydrolyzes peptide bonds involving the carboxyl group of an hydrophobic amino acid.

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