Further Inhibition Studies on Guanidinobenzoatase, a Trypsin-Like Enzyme Associated with Tumour Cells
- 1 January 1987
- journal article
- research article
- Published by Taylor & Francis in Journal of Enzyme Inhibition
- Vol. 1 (3) , 187-201
- https://doi.org/10.3109/14756368709020116
Abstract
Guanidinobenzoatase is a proteolytic enzyme capable of degrading fibronectin and is a tumour associated enzyme. Guanidinobenzoatase has been shown to be an arginine selective protease and is distinct from trypsin, plasminogen activator, plasmin, thrombin and a newly described tumour associated enzyme specific for guanidino phenylalanine residues. These conclusions have been derived from inhibition studies employing 4-methyl-p-guanidinobenzoate as substrate. Three active site titrants for trypsin have been shown to be good substrates for guanidinobenzoatase. A new active site titrant for trypsin, rhodamine bisguanidinobenzoate, can also be used to assay guanidinobenzoatase in a stoichiometric manner. This active site titrant can be employed to label guanidinobenzoate on the surface of leukaemia cells.Keywords
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