Yamaguchi N, Koyama K, Otsuji E, Imanishi J
Département de Microbiologie et Médecine Préventive, Université Médicale de la Préfecture de Kyoto, Japon.
C R Seances Soc Biol Fil. 1989;183(1):79-84.
The activity of cathepsin L is examined in the culture supernatants of 38 human, murine and hamster tumor cell lines. It is found that all cell lines secrete the enzyme possessing cathepsin L activity. The supernatant of HPC-YP cell cultures is purified and characterized as the enzyme preparation, because this supernatant shows the highest cathepsin L activity. The results indicate that the enzyme produced in HPC-YP cells is different from cathepsin L of normal liver in the several points. The molecular weight of the enzyme is 68 kd, whereas it is 34 kd for the liver cathepsin L. The enzyme is more stable to heat treatment and at the various pH than the liver cathepsin L. Furthermore, the inhibitors, which inhibit the liver cathepsin L activity, do not inhibit the activity of this enzyme. It is concluded that the enzyme showing cathepsin L activity in the culture supernatants of human tumor cells is different from human normal liver cathepsin L.
在38种人、小鼠和仓鼠肿瘤细胞系的培养上清液中检测了组织蛋白酶L的活性。发现所有细胞系均分泌具有组织蛋白酶L活性的酶。HPC - YP细胞培养物的上清液被纯化并鉴定为酶制剂，因为该上清液显示出最高的组织蛋白酶L活性。结果表明，HPC - YP细胞产生的酶在几个方面与正常肝脏的组织蛋白酶L不同。该酶的分子量为68kd，而肝脏组织蛋白酶L的分子量为34kd。与肝脏组织蛋白酶L相比，该酶在热处理和不同pH值下更稳定。此外，抑制肝脏组织蛋白酶L活性的抑制剂对该酶的活性没有抑制作用。得出的结论是，人肿瘤细胞培养上清液中显示组织蛋白酶L活性的酶与人类正常肝脏组织蛋白酶L不同。
