Steven F S, Griffin M M, Freemont A J, Johnson J
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, U.K.
J Enzyme Inhib. 1988;2(2):117-27. doi: 10.3109/14756368809040717.
Guanidinobenzoatase is a proteolytic enzyme capable of degrading fibronectin and is a tumour associated enzyme. 9-Aminoacridine is a competitive inhibitor of this enzyme and has been used to locate cells possessing this enzyme in wax embedded sections by means of fluorescent microscopy. Naturally occurring inhibitors of guanidinobenzoatase can be extracted from different tissues. These inhibitors show selectivity in their ability to inhibit the binding of 9-aminoacridine to different types of tumour cells which have invaded human liver tissue. Inhibition is non-competitive and reversible. The results indicate that guanidinobenzoatase exists in a number of different forms on the surface of different tumour cells. These different forms of the enzyme were recognised by inhibitors obtained from different organs. It is suggested that these inhibitors may have a regulatory role in tumour cell migration.
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。9-氨基吖啶是这种酶的竞争性抑制剂，已被用于通过荧光显微镜在石蜡包埋切片中定位含有这种酶的细胞。胍基苯甲酸酶的天然抑制剂可以从不同组织中提取。这些抑制剂在抑制9-氨基吖啶与侵入人肝组织的不同类型肿瘤细胞结合的能力上表现出选择性。抑制作用是非竞争性且可逆的。结果表明，胍基苯甲酸酶以多种不同形式存在于不同肿瘤细胞表面。这些不同形式的酶可被从不同器官获得的抑制剂识别。有人提出这些抑制剂可能在肿瘤细胞迁移中起调节作用。
