| Autor: |
Scott, R. P., Ninjoor, V., Srivastava, P. N. |
| Zdroj: |
Reproduction; January 1987, Vol. 79 Issue: 1 p67-74, 8p |
| Abstrakt: |
Summary.Cathepsin B (EC 3.4.22.1) has been purified from rabbit testes to apparent homogeneity by chromatography on DE-52, affinity chromatography on organomercurial agarose and subsequent gel filtrations on Sephadex G-75. The enzyme is composed of a single polypeptide of Mr23 000. Thiol blocking agents and leupeptin abolished the activity of the enzyme completely. The enzyme showed maximum activity at pH 6·0 and 43°C, required 2 mm-cysteine for the optimal activity and had a Km1·45 × 10−3musing Z-Arg-β-naphthylamide as the substrate. However, Z-Arg-Arg-β-naphthylamide was 12 times more sensitive as a substrate than was Z-Arg-β-naphthylamide. Rabbit testicular cathepsin B hydrolysed intact proteins. An endogenous inhibitor isolated from the rabbit testes inhibited purified Cathepsin B. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
