Kregar I, Locnikar P, Popović T, Suhar A, Lah T, Ritonja A, Gubensek F, Turk V
Acta Biol Med Ger. 1981;40(10-11):1433-8.
Cathepsins B, H and S were isolated from bovine lymph nodes and bovine spleen. It was shown that the incubation of homogenate at 37 degrees C at acid pH increased the total BANA hydrolase activity and LeuNA activity, whereas it decreased the total activity of cathepsin S. All three enzymes are electrophoretically homogeneous and probably composed of a single polypeptide chain. They exist in multiple forms as shown by isoelectric focusing. Far UV CD spectra revealed a rather high percentage of unordered structure. The three cysteine proteinases were inhibited by thiol blocking reagents, leupeptin and by an inhibitor isolated from Vipera ammodytes venom. Results on the specificity toward various substrates and the influence of pH on enzymatic activity are presented.
组织蛋白酶B、H和S从牛淋巴结和牛脾脏中分离得到。结果表明，在酸性pH值下于37℃孵育匀浆会增加总的BANA水解酶活性和亮氨酸萘胺酶活性，而组织蛋白酶S的总活性则会降低。所有这三种酶在电泳上均为均一的，可能由一条单一的多肽链组成。如等电聚焦所示，它们以多种形式存在。远紫外圆二色光谱显示无序结构的比例相当高。这三种半胱氨酸蛋白酶受到硫醇封闭试剂、亮抑酶肽以及从极北蝰蛇毒液中分离出的一种抑制剂的抑制。文中给出了对各种底物的特异性以及pH对酶活性影响的结果。
