Steven F S, Griffin M M, Wong T L, Yasmin R, Mangel W F
Department of Biochemistry, University of Manchester, UK.
J Enzyme Inhib. 1987;1(3):187-201. doi: 10.3109/14756368709020116.
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.
胍基苯甲酸酶是一种能够降解纤连蛋白的蛋白水解酶，是一种肿瘤相关酶。胍基苯甲酸酶已被证明是一种精氨酸选择性蛋白酶，与胰蛋白酶、纤溶酶原激活剂、纤溶酶、凝血酶以及一种新描述的对胍基苯丙氨酸残基具有特异性的肿瘤相关酶不同。这些结论来自于以4-甲基-对-胍基苯甲酸酯为底物的抑制研究。已证明三种胰蛋白酶活性位点滴定剂是胍基苯甲酸酶的良好底物。一种新的胰蛋白酶活性位点滴定剂，罗丹明双胍基苯甲酸酯，也可用于以化学计量方式测定胍基苯甲酸酶。这种活性位点滴定剂可用于标记白血病细胞表面的胍基苯甲酸酯。
