AMP-deaminase from human term placenta was chromatographed on a phosphocellulose column and physico-chemical and immunological properties of the purified enzyme were investigated. At physiological pH 7.0, in the absence of regulatory ligands (control conditions) studied AMP-deaminase manifested sigmoid-shaped substrate saturation kinetics, with half-saturation parameter (S0.5) value of about 7 mM. Addition of important allosteric effectors (ATP, ADP or orthophosphate) modified kinetic properties of studied AMP-deaminase, influencing mainly the value of S0.5, parameter. Micromolar concentrations of stearylo-CoA inhibited potently the enzyme making it no longer sensitive towards 1 mM ATP-induced activation. SDS-PAGE electrophoresis of the purified enzyme revealed presence of 68 kDa protein fragment, reacting with anti-(human) liver AMP-deaminase antibodies. Experimental results presented indicate that 'liver type' of AMP-deaminase is an enzyme form present in human term placenta.

译文

人足月胎盘的AMP-脱氨酶在磷酸纤维素柱上进行色谱分离,并研究了纯化酶的理化和免疫学特性。在生理pH 7.0下,在没有调节配体的情况下 (对照条件),研究了AMP-脱氨酶表现出乙状状底物饱和动力学,半饱和参数 (S0.5) 值约为7毫米。添加重要的变构效应子 (ATP,ADP或正磷酸盐) 修饰了所研究的AMP-脱氨酶的动力学特性,主要影响参数S0.5的值。微摩尔浓度的硬脂酰辅酶a有效抑制了该酶,使其不再对1毫米ATP诱导的活化敏感。纯化酶的sds-page电泳显示存在68 kDa蛋白片段,与抗 (人) 肝腺苷酸脱氨酶抗体反应。实验结果表明,AMP-脱氨酶的 “肝型” 是人期胎盘中存在的一种酶形式。

+1
+2
100研值 100研值 ¥99课程
检索文献一次
下载文献一次

去下载>

成功解锁2个技能,为你点赞

《SCI写作十大必备语法》
解决你的SCI语法难题!

技能熟练度+1

视频课《玩转文献检索》
让你成为检索达人!

恭喜完成新手挑战

手机微信扫一扫,添加好友领取

免费领《Endnote文献管理工具+教程》

微信扫码, 免费领取

手机登录

获取验证码
登录