Hirschman A, Hirschman M
Enzyme. 1977;22(1):2-12. doi: 10.1159/000458500.
Extracts of epiphyseal articular and costal cartilages and of metaphyseal bone showed different profiles of activity against 21 aminoacyl beta-naphthylamides. Except for the activity against arginyl and lysyl beta-naphthylamides, most of the activities required the presence of Triton X-100 for extraction, suggesting that in situ, the enzymes are bound to or within membranous structures. Histochemical studies demonstrated that most, if not all, activity was intracellular. The activity is enhanced by Co2+. TAME (2 X 10(-4) mol/l) inhibits activity against leucyl beta-naphthylamide and some others, but has little, if any, inhibition of activity against alanyl beta-naphthylamide. Gel filtration of the extract showed a high molecular weight active fraction eluting with proteoglycan, and an active fraction with an approximate molecular weight of about 230,000. Two active fractions are obtained by gradient elution from DEAE-cellulose.
骨骺关节软骨、肋软骨及干骺端骨的提取物对21种氨酰基β-萘酰胺表现出不同的活性谱。除了对精氨酰和赖氨酰β-萘酰胺的活性外，大多数活性在提取时需要Triton X-100的存在，这表明在原位，酶与膜结构结合或存在于膜结构内。组织化学研究表明，大部分（如果不是全部的话）活性是细胞内的。Co2+可增强该活性。TAME（2×10(-4)mol/l）抑制对亮氨酰β-萘酰胺及其他一些物质的活性，但对丙氨酰β-萘酰胺的活性几乎没有抑制作用（如果有抑制作用的话也很小）。提取物的凝胶过滤显示，一个高分子量活性级分与蛋白聚糖一起洗脱，另一个活性级分的近似分子量约为230,000。通过从DEAE-纤维素进行梯度洗脱可得到两个活性级分。
