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α-胰凝乳蛋白酶原A与烷基脲的相互作用。

Interactions of alpha-chymotrypsinogen A with alkylureas.

作者信息

Poklar N, Vesnaver G, Lapanje S

机构信息

Department of Chemistry, University of Ljubljana, Slovenia.

出版信息

Biophys Chem. 1996 Jan;57(2-3):279-89. doi: 10.1016/0301-4622(95)00073-1.

Abstract

Solvation of alpha-chymotrypsinogen A (alpha-ctg A) in aqueous urea, methylurea, N,N'-dimethylurea and ethylurea was studied by density measurements. From the densities at constant molality and at constant chemical potential the preferential solvation parameters were determined. In urea and methylurea preferential solvation was observed, whereas in N,N'-dimethylurea and ethylurea at higher concentration water is preferentially bound. From preferential solvation data Gibbs free energy of transfer of alpha-ctg A from water to urea and alkylurea solutions were calculated. Since the enthalpies of transfer were determined previously, the entropies of transfer could also be obtained so that a complete thermodynamic description is available. An attempt is made to interpret the values of the thermodynamic quantities in terms of various interactions involved in solvation as well as to calculate the exchange constant by using the model of weak interactions. In solvation of alkylureas the hydrophobic nature of the alkyl groups is clearly reflected.

摘要

通过密度测量研究了α-胰凝乳蛋白酶原A(α-ctg A)在尿素水溶液、甲基脲、N,N'-二甲基脲和乙基脲中的溶剂化作用。根据恒定质量摩尔浓度和恒定化学势下的密度确定了优先溶剂化参数。在尿素和甲基脲中观察到优先溶剂化,而在较高浓度的N,N'-二甲基脲和乙基脲中,水优先结合。根据优先溶剂化数据计算了α-ctg A从水转移到尿素和烷基脲溶液中的吉布斯自由能。由于先前已确定转移焓,因此也可以获得转移熵,从而得到完整的热力学描述。尝试根据溶剂化中涉及的各种相互作用来解释热力学量的值,并使用弱相互作用模型计算交换常数。在烷基脲的溶剂化过程中,烷基的疏水性质得到了明显体现。

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