Barkhudarian N A, Azarian A V, Akopian T N, Buniatian G Kh
Ukr Biokhim Zh (1978). 1981 Nov-Dec;53(6):36-9.
Six peaks of the endopeptidase activity at pH 3.2 were obtained after isoelectric focusing of soluble fractions of cortex and hypothalamus of the human brain. The molecular weight of these endopeptidases are approximately 50000. All obtained endopeptidases possess almost the same Km and I50 relative to the substrate--pyridoxal globin and specific inhibitor--pepstatin. The studies of the revealed properties show that the endopeptidases are multiple forms of cathepsin D.
对人脑皮质和下丘脑可溶部分进行等电聚焦后,在pH 3.2条件下获得了六种内肽酶活性峰。这些内肽酶的分子量约为50000。所有获得的内肽酶相对于底物吡哆醛球蛋白和特异性抑制剂胃蛋白酶抑制剂具有几乎相同的Km和I50。对所揭示特性的研究表明,这些内肽酶是组织蛋白酶D的多种形式。