Guinec N, Dalet-Fumeron V, Pagano M
Laboratoire de biochimie, faculté de médecine Broussais Hôtel-Dieu, université Pierre-et-Marie-Curie, Paris, France.
Bull Cancer. 1993 Jan;80(1):55-61.
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. The basement membrane used for these experiments is the bovine lens capsule (weight approximately 50 mg). Papain inactivated by E64 was used in competition experiments, that made it possible to obtain the equilibrium constant, Kd and the number of substrate sites per capsule, n. Values were found around 10(-7) M for Kd, and in the 10(12) range for n. 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.
通过利用这些蛋白酶对其特定荧光底物的酶活性，研究了木瓜蛋白酶超家族的半胱氨酸蛋白酶（木瓜蛋白酶和组织蛋白酶B、B样和L）与基底膜的结合。用于这些实验的基底膜是牛晶状体囊（重量约50毫克）。在竞争实验中使用了被E64灭活的木瓜蛋白酶，这使得能够获得平衡常数Kd和每个囊的底物位点数量n。发现Kd值约为10^(-7) M，n值在10^(12)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。
