Rakitzis E T, Malliopoulou T B
Biochem J. 1976 Mar 1;153(3):737-9. doi: 10.1042/bj1530737.
Cathepsin D, purified from bovine spleen, is inactivated by the unstable inhibitors dithiophosgene and 2,2-dichloro-1,3-dithiacyclobutanone. Inhibition constants are identical for both of the compounds tested: Ki 96.1 muM;k/c0.406. It appears that the active species is 2,2-dichloro-1,3-dithiacyclobutanone, to which dithiophosgene is hydrolysed before cathepsin D inactivation.
从牛脾脏中纯化得到的组织蛋白酶D可被不稳定抑制剂二硫代光气和2,2-二氯-1,3-二硫杂环丁烷灭活。所测试的两种化合物的抑制常数相同：Ki为96.1 μM；k/c为0.406。似乎活性物质是2,2-二氯-1,3-二硫杂环丁烷，在组织蛋白酶D失活之前，二硫代光气会水解成该物质。
