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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 24 print issues and online access
$259.00 per year
only $10.79 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
Rights and permissions
About this article
Cite this article
Short, A., Steven, F., Griffin, M. et al. β-Naphthylamidase activity of the cell surface of Ehrlich ascites cells. Reversible control of enzyme activity by metal ions and thiols. Br J Cancer 44, 709–716 (1981). https://doi.org/10.1038/bjc.1981.257
Issue Date:
DOI: https://doi.org/10.1038/bjc.1981.257
This article is cited by
-
Collagenolytic mechanisms in tumor cell invasion
Cancer and Metastasis Review (1984)