Murachi T
Biochem Soc Symp. 1984;49:149-67.
There are two forms of Ca2+-dependent cysteine proteinase: low Ca2+ (microM concentration)-requiring calpain I and high Ca2+ (mM concentration)-requiring calpain II. We have recently succeeded in establishing an efficient method for isolating calpains I and II from several tissues and also a method for separating the heavy (80 kDa) and light (30 kDa) subunits from a calpain molecule. These methods enabled us to obtain a variety of calpains I and II and their subunit proteins each in a highly pure state so that these proteins can be compared physically, chemically and immunologically. Calpastatin, a calpain-specific endogenous inhibitor protein, was also purified and characterized. Although the intercellular localization of calpains I and II is being elucidated by use of the respective monospecific antibodies, the true biological functions of calpain and calpastatin still remain rather obscure.
需要低钙(微摩尔浓度)的钙蛋白酶I和需要高钙(毫摩尔浓度)的钙蛋白酶II。我们最近成功建立了一种从多种组织中分离钙蛋白酶I和II的有效方法,以及一种从钙蛋白酶分子中分离重(80 kDa)和轻(30 kDa)亚基的方法。这些方法使我们能够以高纯度获得各种钙蛋白酶I和II及其亚基蛋白,从而可以对这些蛋白进行物理、化学和免疫学比较。钙蛋白酶特异性内源性抑制蛋白钙蛋白酶抑制蛋白也得到了纯化和表征。尽管通过使用各自的单特异性抗体正在阐明钙蛋白酶I和II的细胞内定位,但钙蛋白酶和钙蛋白酶抑制蛋白的真正生物学功能仍然相当模糊。