Lapresle C, Puizdar V, Porchon-Bertolotto C, Joukoff E, Turk V
Biol Chem Hoppe Seyler. 1986 Jun;367(6):523-6. doi: 10.1515/bchm3.1986.367.1.523.
Rabbit cathepsins D and E were isolated from bone marrow. Both enzymes were purified by affinity chromatography on pepstatin-Sepharose 4B and Con A-Sepharose 4B. Purity of the enzymes was ascertained by two-dimensional gel electrophoresis after iodination. The isoelectric point of cathepsin D was found to be 6.95. Cathepsin E was shown to consist of two subunits having molecular masses each of 40 kDa and isoelectric points of 4.60 and 4.65, respectively. The amino-acid composition of cathepsin E was found to be different from that of cathepsin D.
兔组织蛋白酶D和E是从骨髓中分离出来的。两种酶都通过在胃蛋白酶抑制剂-琼脂糖4B和刀豆球蛋白A-琼脂糖4B上的亲和层析进行纯化。碘化后通过二维凝胶电泳确定酶的纯度。发现组织蛋白酶D的等电点为6.95。组织蛋白酶E显示由两个亚基组成,每个亚基的分子量为40 kDa,等电点分别为4.60和4.65。发现组织蛋白酶E的氨基酸组成与组织蛋白酶D不同。