Further inhibition studies on guanidinobenzoatase, a trypsin-like enzyme associated with tumour cells.
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.
Steven
F S
FS
Department of Biochemistry, University of Manchester, UK.
Griffin
M M
MM
Wong
T L
TL
Yasmin
R
R
Mangel
W F
WF
D000818:Animals; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors*; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology; D010450:Endopeptidases; D007700:Kinetics; D051379:Mice; D011480:Protease Inhibitors / Q000494:pharmacology*; D014357:Trypsin
D011480:Protease Inhibitors; D002265:Carboxylic Ester Hydrolases; C037288:guanidinobenzoate esterase; D010450:Endopeptidases; D014357:Trypsin