磁化过氧化氢酶的稳定性研究及其机理初探  

STUDIES ON STABILITY OF MAGNETIZED CATALASE AND AN INITIAL ANALYSIS OF ITS MACHANISM

作　　者：张军[1] 孙凡[2] 陈德万[2] 李光林[2] 

机构地区：[1]重庆医科大学基础医学学院,重庆400016 [2]西南农业大学基础科技学院,重庆400716

出　　处：《西南农业大学学报（自然科学版）》2001年第3期273-275,共3页Journal of Southwest Agricultural University

摘　　要：研究了经 0 .2 3T～ 0 .6 1T磁场处理 1h所得磁化过氧化氢酶 (CAT)的滞后活力、紫外差光谱及荧光发射光谱的变化。磁化酶在放置过程中 ,活力下降慢于天然酶 ,相对活力随滞后时间的延长而增加 ,活力变化曲线的线型随磁感应强度增加而呈现规律性变化。在滞后期间内 ,磁化酶紫外差光谱连续变化 ,荧光发射光谱λ 330nm发射峰位未移动 ,而荧光发射强度下降。研究表明 ,磁化酶稳定性增加 ,其变性失活的构象变化过程明显不同于天然酶。同时 ,初步分析了磁化酶稳定性增加的机理。The hyteretic relative activity, ultraviolet differential spectra and fluorescence emission spectra of magnetized catalase exposed to 0.23～0.61T magnetic field for 1 hour were studied. When allowed to stand in a non-magnetic environment, the magnetized enzyme activity dropped more slowly than that of the natural enzyme, the relative activity of the magnetized enzyme tended to grow and the types of enzymatic activity curves showed regular changes. During the hysteretic period the ultraviolet differential spectra changed continuously, the location of fluorescence emission peak was not shifted, but its relative fluorescence intensity decreased. Such results indicated that the stability of the magnetized enzyme rose in contrast with the natural enzyme, and the process of its inactivation caused by conformational changes were distinctly different from those of the natural enzyme. The possible mechanism for the increase in the stability of the magnetic enzyme is discussed in the present paper.

关 键 词：过氧化氢酶 磁场 稳定性 机理 

分 类 号：Q554.6[生物学—生物化学]