Diez A, Campo M L, Soler G
Departmento de Bioquimica y Biologia Molecular y Genética, Facultad de Veterinaria, Universidad de Extremadura, Cáceres, Spain.
Biotechnol Appl Biochem. 1990 Jun;12(3):237-44.
Rat liver arginase was covalently trapped in a fibrin clot. Among the physicochemical properties of the enzyme studied were Mn2+ requirement, pH behavior, temperature and time stability, effect of denaturing agents, and kinetic properties. The immobilized arginase showed the same substrate affinity as soluble arginase, but had higher stability at room temperature, was more resistant to denaturation, and had a higher catalytic activity at physiological pH. The properties so far examined may enhance the use of immobilized arginase in cancer therapy.
大鼠肝脏精氨酸酶被共价固定在纤维蛋白凝块中。所研究的该酶的物理化学性质包括对Mn2+的需求、pH行为、温度和时间稳定性、变性剂的影响以及动力学性质。固定化精氨酸酶表现出与可溶性精氨酸酶相同的底物亲和力，但在室温下具有更高的稳定性，更耐变性，并且在生理pH下具有更高的催化活性。目前所检测的这些性质可能会促进固定化精氨酸酶在癌症治疗中的应用。
