Further inhibition studies on guanidinobenzoatase, a trypsin-like enzyme associated with tumour cells |
| |
Authors: | F S Steven M M Griffin T L Wong R Yasmin W F Mangel |
| |
Affiliation: | Department of Biochemistry, University of Manchester, UK. |
| |
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: | |
|
|