Pontremoli S, Melloni E, Damiani G, Michetti M, Salamino F, Sparatore B, Horecker B L
Arch Biochem Biophys. 1984 Aug 15;233(1):267-71. doi: 10.1016/0003-9861(84)90625-8.
A monoclonal antibody raised against rabbit liver cathepsin M binds to intact rabbit liver lysosomes. The binding is specific and is abolished by treating the lysosomes with trypsin, which has previously been shown to digest the membrane-bound cathepsin M [S. Pontremoli, E. Melloni, M. Michetti, F. Salamino, B. Sparatore, and B. L. Horecker (1982) Biochem, Biophys. Res. Commun. 106, 903-909]. Rabbit liver lysosomes are adsorbed onto Sepharose 4B coupled to anti-cathepsin M, but not to Sepharose 4B itself or to Sepharose coupled to a nonspecific antibody. The results confirm the location of membrane-bound cathepsin M on the outer surface of the lysosomal membrane.
一种针对兔肝组织蛋白酶M产生的单克隆抗体可与完整的兔肝溶酶体结合。这种结合具有特异性，用胰蛋白酶处理溶酶体后结合作用消失，此前研究表明胰蛋白酶可消化膜结合的组织蛋白酶M [S. 庞特雷莫利、E. 梅洛尼、M. 米凯蒂、F. 萨拉米诺、B. 斯帕拉托雷和B. L. 霍雷克 (1982年) 《生物化学与生物物理学研究通讯》106, 903 - 909]。兔肝溶酶体可吸附到偶联抗组织蛋白酶M的琼脂糖4B上，但不能吸附到琼脂糖4B本身或偶联非特异性抗体的琼脂糖上。这些结果证实了膜结合组织蛋白酶M位于溶酶体膜的外表面。
