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附着于水不溶性颗粒和薄片上的乳酸脱氢酶的制备及其动力学

The preparation and kinetics of lactate dehydrogenase attached to water-insoluble particles and sheets.

作者信息

Wilson R J, Kay G, Lilly M D

出版信息

Biochem J. 1968 Aug;108(5):845-53. doi: 10.1042/bj1080845.

Abstract
  1. The preparation of lactate dehydrogenase covalently attached to anion-exchange cellulose particles and sheets by use of a dichloro-sym-triazinyl dyestuff, Procion brilliant orange MGS, is described. 2. The stability and kinetic properties of these preparations were investigated. 3. An equation is derived to describe the change in concentration of a substrate when passed through a uniform bed of a substrate-inhibited enzyme. A number of theoretical curves are shown to illustrate the system. 4. A titrimetric assay for lactate dehydrogenase is described, and shown to be stoicheiometric over the range pH5.0-9.2. 5. The results are discussed in relation to previous work, and the effects of charged groups on the support, and of the diffusion film surrounding any particle in suspension, are treated qualitatively.
摘要
  1. 描述了使用二氯 - 对称 - 三嗪基染料Procion亮橙MGS将乳酸脱氢酶共价连接到阴离子交换纤维素颗粒和薄片上的制备方法。2. 研究了这些制剂的稳定性和动力学性质。3. 推导了一个方程来描述底物通过底物抑制酶的均匀床层时浓度的变化。展示了一些理论曲线来说明该系统。4. 描述了一种乳酸脱氢酶的滴定测定法,并表明在pH5.0 - 9.2范围内是化学计量的。5. 结合先前的工作对结果进行了讨论,并定性地探讨了载体上带电基团以及悬浮液中任何颗粒周围扩散膜的影响。

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[Inhibition of lactate dehydrogenase by nicotinamide adenine dinucleotide].
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本文引用的文献

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A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS.一种用于蛋白质定量的微量双缩脲法。
Anal Biochem. 1964 Dec;9:401-10. doi: 10.1016/0003-2697(64)90200-3.

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