BINDING-STUDIES ON 3'-CYTIDIN MONOPHOSPHATE AND RIBONUCLEASE A DERIVATIVES BY FLOW AND BATCH CALORIMETRY

被引：8

作者：

BATTISTEL, E ^{[1
]}

SABBIONETA, P ^{[1
]}

RIALDI, G ^{[1
]}

机构：

[1] CNR,CTR STUDI CHIM FIS MACROMOLEC SINTETICHE & NATURALI,I-16132 GENOA,ITALY

来源：

THERMOCHIMICA ACTA | 1990年 / 172卷

关键词：

D O I：

10.1016/0040-6031(90)80556-E

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

Isothermal batch calorimetry can give useful information on the biological activity of enzymes immobilized on solid supports. As a model system, the enthalpy change and the apparent equilibrium constant of the cytidine-3'-monophosphate binding to soluble ribonuclease A were evaluated with the batch and flow calorimeters and the results compared. The batch technique was then employed to study the same thermodynamic parameters with ribonuclease immobilized on Silica beads. Reproducible results were obtained after correction of the thermograms for the instrumental time response delay. © 1990.

引用

页码：21 / 30

页数：10