Bird J W, Schwartz W N, Spanier A M
Acta Biol Med Ger. 1977;36(11-12):1587-604.
Cathepsin B and cathepsin D were purified from rat liver and skeletal muscle. Electrophoretic analyses revealed that the enzymes were highly purified, and isoelectric focusing demonstrated multiple forms of both enzymes. Purified actin and myosin, as well as actin and myosin in myofilaments and myofibrils, were degraded by the purified cathepsins B and D. Degradation of myosin was completely blocked by the cathepsin B and D inhibitors, leupeptin and pepstatin, respectively. Cathepsins B and D were visualized by electron microscopy, using CBZ-Ala- Arg-Arg-4-methoxy-beta-naphthylamine and BZ-Arg-Gly-Phe-Leu-4-methoxy-beta-naphthylamine as substrates.
组织蛋白酶B和组织蛋白酶D从大鼠肝脏和骨骼肌中纯化得到。电泳分析表明这些酶已高度纯化，等电聚焦显示这两种酶均有多种形式。纯化的肌动蛋白和肌球蛋白，以及肌丝和肌原纤维中的肌动蛋白和肌球蛋白，均被纯化的组织蛋白酶B和D降解。肌球蛋白的降解分别被组织蛋白酶B和D的抑制剂亮抑蛋白酶肽和胃酶抑素完全阻断。以CBZ-丙氨酰-精氨酰-精氨酰-4-甲氧基-β-萘胺和BZ-精氨酰-甘氨酰-苯丙氨酰-亮氨酰-4-甲氧基-β-萘胺作为底物，通过电子显微镜观察到了组织蛋白酶B和D。
