刷状缘水解酶的Triton和胰蛋白酶形式的催化及调节特性。
Catalytic and regulatory properties of the Triton and trypsin forms of the brush border hydrolases.
作者信息
Ugolev A M, Mityushova N M, Egorova V V, Gozite I K, Koltushkina G G
出版信息
Gut. 1979 Sep;20(9):737-42. doi: 10.1136/gut.20.9.737.
Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila. Differences in the catalytic propertiis of the two enzyme forms were demonstrated, which suggested that the hydrophobic part of the enzyme was involved in maintaining optimal conformation of the catalytic part. Many modifiers have beenfound to influence the Triton rather than the trypsin form of the enzyme. It is therefore suggested that the hydrophobic sub-units of the enzymes might be involved in transmitting information from the cytoplasm into the external surface of the membrane, the cell in this way regulating the activity of surface enzymes. If this is indeed the case, it is suggested that the hydrophobic part performs functions not only of external but also of internal regulation.
两亲性酶，即转化酶（EC 3.2.1.26）、β-淀粉酶（EC 3.2.1.3）和碱性磷酸酶（EC 3.1.3.1），从大鼠小肠黏膜中以胰蛋白酶形式和 Triton 形式纯化得到，对其催化和调节特性在大鼠和果蝇中进行了比较。证明了两种酶形式在催化特性上存在差异，这表明酶的疏水部分参与维持催化部分的最佳构象。已发现许多调节剂对酶的 Triton 形式而非胰蛋白酶形式有影响。因此有人提出，酶的疏水亚基可能参与将信息从细胞质传递到膜的外表面，细胞以此方式调节表面酶的活性。如果确实如此，有人提出疏水部分不仅执行外部调节功能，还执行内部调节功能。
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