Abstract
1. 1. Catheptic activity, measured by the hydrolysis of hemoglobin, increased remarkably during metamorphosis in the tadpole tail of Rana catesbeiana. 2. 2. Pepstatin inhibited about 75% of the catheptic activity, and the combination of pepstatin and monoiodoacetate inhibited it completely. Leupeptin slightly inhibited catheptic activity. 3. 3. By gel chromatography on Sephadex G-100, three molecular forms of catheptic activity were obtained. Their molecular weights were: Fraction I—larger than 100,000, Fraction II—50,000 and Fraction III—32,000. 4. 4. Fraction II, showing the highest activity was strongly inhibited by pepstatin and assumed to be cathepsin D. Fraction III was strongly inhibited by monoiodoacetate, indicating the existence of SH-proteinase.
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