艾氏腹水癌细胞表面的β-萘基酰胺酶活性。金属离子和硫醇对酶活性的可逆调控。
beta-Naphthylamidase activity of the cell surface of Ehrlich ascites cells. Reversible control of enzyme activity by metal ions and thiols.
作者信息
Short A K, Steven F S, Griffin M M, Itzhaki S
出版信息
Br J Cancer. 1981 Nov;44(5):709-16. doi: 10.1038/bjc.1981.257.
Abstract
Ehrlich ascites tumour cells grown in mice have a cell-surface trypsin-like neutral protease (TLNP) which is not inhibited by high-mol.-wt inhibitors of trypsin. This enzyme is inhibited by low concentrations of zinc, which may be removed by chelating agents, with the consequent return of enzymic activity. Gold, provided as the drugs aurothiomalate or auranofin, also inhibits TLNP. The gold can be removed from the enzyme by incremental addition of thiols. The mechanisms of gold transfer to the active site to cause inhibition and subsequent removal of gold with reactivation of TLNP, have been shown to be controlled by reversible thiol-exchange reactions.
摘要
在小鼠体内生长的艾氏腹水癌细胞具有一种细胞表面类胰蛋白酶中性蛋白酶（TLNP），该酶不受高分子量胰蛋白酶抑制剂的抑制。低浓度的锌可抑制这种酶，螯合剂可去除锌，从而使酶活性恢复。作为药物的硫代苹果酸金钠或金诺芬所提供的金，也能抑制TLNP。通过逐步添加硫醇可将金从酶中去除。已证明金转移到活性位点导致抑制以及随后去除金使TLNP重新激活的机制受可逆硫醇交换反应控制。
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