纯化减少的尼古丁胺胺氨基二核酸:对三种细胞来源的乳酸脱酶异酶的反应
Science (New York, N.Y.)
|May 1, 1981
概括
乳酸脱酶 (LDH) 异酶对纯化的NADH表现出不同的反应,这表明分子差异,而不仅仅是组成,影响抑制剂的敏感性. 商业NADH含有影响LDH活性的抑制剂.
科学领域:
- 生物化学 生物化学
- 酶学 是一种酶学.
- 细胞生物学 细胞生物学
背景情况:
- 乳酸脱酶 (LDH) 异酶是细胞代谢中的关键酶.
- LDH异酶活性的变化与不同的细胞类型和疾病状态有关.
- LDH异酶的活性可以受到辅酶制剂的影响,特别是减少的尼古丁胺胺氨基二核酸 (NADH).
研究的目的:
- 研究来自各种细胞源的LDH异酶对净化与商业NADH的差异反应.
- 要确定单独的异酶组成是否解释了所观察到的酶活性变化.
- 阐明商业NADH制剂中存在的抑制剂对LDH异酶功能的作用.
主要方法:
- 从子红细胞,控制肝细胞和化学转化细胞中净化乳酸脱酶 (LDH) 异酶.
- 根据特定标准制备和净化减少的尼古丁胺氨酸二核酸 (NADH),确保不受抑制剂的影响.
- 使用净化和商业NADH制剂对LDH异酶活性进行比较分析.
- 在商业NADH制剂中识别斯特兰德-克莱森抑制剂.
主要成果:
- 来自子红细胞的LDH-1与无抑制剂的NADH一起表现出最大的活性增加.
- 来自控制肝细胞的LDH异酶与纯化的NADH显示了中度刺激.
- 来自化学转换细胞的LDH异酶对净化NADH的反应很小.
- 商业NADH制剂含有Strandjörd-Clayson抑制剂,这些抑制剂显著影响LDH活性.
- 单独的异酶成分并不能完全解释观察到的差异性反应.
结论:
- 个体LDH异酶内部的特定分子差异有助于它们对NADH制剂的多样性反应.
- 在商业NADH中存在Strandjörd-Clayson抑制剂显著影响LDH活性.
- 了解这些分子差异对于准确评估生物系统中的LDH功能至关重要.
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