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Equilibrium Constants of Interaction between Pyridoxal-5'-Phosphate Coenzyme and Glycine and Its Oligopeptides in Aqueous Buffered Saline
Russian Journal of Physical Chemistry A ( IF 0.7 ) Pub Date : 2020-10-30 , DOI: 10.1134/s0036024420110035
V. P. Barannikov , E. A. Venediktov

Abstract

Electronic absorption spectroscopy is used to study the patterns of bonding of oligopeptides of glycyl-glycine and glycyl-glycyl-glycine using the coenzyme pyridoxal-5'-phosphate at 293 K in a phosphate buffer solution at pH 7.35. The results are compared to the similar process for monomeric glycine. The interaction constants and the spectral parameters of the reaction products are determined. The observed increase in the peptide–coenzyme bonding equilibrium constants in the Gly–(Gly–Gly)–(Gly–Gly–Gly) series is due to a drop in the basicity of the reaction’s amino group and an increase in the proportion of peptides with non-ionized amino groups in the solution. An increase in the chain length of the peptide is accompanied by a reduction in the coefficient of extinction of the resulting Schiff base.



中文翻译:

缓冲盐水中吡y醛-5'-磷酸辅酶与甘氨酸及其寡肽相互作用的平衡常数

摘要

电子吸收光谱法用于研究在pH值为7.35的磷酸盐缓冲溶液中在293 K下使用辅酶吡al醛5'-磷酸酯对甘氨酰-甘氨酸和甘氨酰-甘氨酰-甘氨酸的寡肽键合的模式。将结果与单体甘氨酸的类似过程进行比较。确定反应产物的相互作用常数和光谱参数。在Gly-(Gly-Gly)-(Gly-Gly-Gly)系列中观察到的肽-辅酶键合平衡常数的增加是由于反应氨基的碱性降低和肽比例的增加溶液中带有非电离氨基。肽链长度的增加伴随着所得席夫碱的消光系数的降低。

更新日期:2020-10-30
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