Guinec N, Dalet-Fumeron V, Pagano M
Laboratoire de Biochimie, Faculté de Médecine Broussais Hotel-Dieu, Université Pierre et Marie Curie, Paris, France.
FEBS Lett. 1992 Aug 24;308(3):305-8. doi: 10.1016/0014-5793(92)81299-2.
Binding of cysteine proteinases of the papain superfamily (papain and cathepsins B, B-like and L) to basement membranes was studied by using the enzymatic activity of these proteinases against their specific fluorogenic substrates. Papain inactivated by E64 was used for Kd determination by competition experiments. The binding was characterized using the following parameters, the equilibrium constant, Kd, and the number of substrate sites, n, values of which were in the range of 10(-7) M and 10(12), respectively. Such results would be of significant interest for the understanding of the biological role of cysteine proteinases in tumour invasion and other types of tissue remodeling.
通过利用木瓜蛋白酶超家族(木瓜蛋白酶、组织蛋白酶B、B样蛋白酶和L)的半胱氨酸蛋白酶对其特定荧光底物的酶活性,研究了这些蛋白酶与基底膜的结合。通过竞争实验,将经E64失活的木瓜蛋白酶用于测定解离常数(Kd)。使用以下参数对结合进行表征:平衡常数Kd和底物位点数量n,其值分别在10^(-7) M和10^(12) 的范围内。这些结果对于理解半胱氨酸蛋白酶在肿瘤侵袭和其他类型组织重塑中的生物学作用具有重要意义。