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从厦门文昌鱼(Branchiostonia belcheri Gary)分离纯化获得聚丙烯酰胺胶电泳单一蛋白区带的酸性磷酸酯酶(EC3.1,3.2)应用化学修饰方法,荧光以及紫外-可见光谱的变化,探讨Trp残基与酶活力的关系,被NBS修饰的Trp基团仅有一个Trp残基被氧化时,酶活力丧失90％,该Trp残基为ACPase表现活力所必需,而且优先被氧化、从光谱扫描(230～600nm)结果表明,经NBS修饰以后的酶构象发生变化,文昌鱼ACPase的Trp残基和酶分子上的铁离子等基团均为酶活力的必需基团,推测两者可能以配位结合,共同维持酶活力中心的构象。
The chemical phosphatase (EC3.1,3.2) isolated from the purified ampicillin gel electrophoresis gel electrophoresis was purified from the branch of Xiamen amphioxus (Branchiostonia belcheri Gary) by chemical modification, fluorescence and UV-Vis spectra, The relationship between the activity of the base and the enzyme, when only one Trp residue of Trp group modified by NBS is oxidized, the activity of the enzyme is lost by 90%. The Trp residue is essential for ACPase to express vitality and is preferentially oxidized. From the spectral scan 230-600nm). The results showed that the enzyme conformation changed after NBS modification. The Trp residues of ACPase and the iron ions in enzyme molecule were all necessary groups for enzyme activity. Combine to jointly maintain the conformation of the enzyme activity center.