Microcalorimetric Studies of the Interactions of Imidazole with Immobilized Cu(II): Effects of pH Value and Salt Concentration

✍ Scribed by Ching-Fa Wu; Wen-Yih Chen; Jiunn-Fwu Lee

• Publisher: Elsevier Science
• Year: 1996
• Tongue: English
• Weight: 116 KB
• Volume: 183
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1996.0538

✦ Synopsis

ions frequently varies with the topography of the protein In this investigation, we measured the influence of pH value surface and the chemistry and physical conditions of the and salt concentration on the heat of interaction between imidazole interaction conditions. Although mechanisms have been proand CS-IDA-Cu(II) gel with a highly sensitive microcaloriposed for IMA with protein, the macromolecular recognition meter. The direct enthalpy measurement of the interaction proof protein by immobilized ions remains unclear. In the provides thermodynamic information regarding the binding behavior posed mechanism (11, 12), the formation of a coordinated of imidazole toward the immobilized metal ion. The changes in complex between a protein and an immobilized metal ion is binding enthalpy with the adsorbed amount of imidazole measured considered to be the major binding mode. However, more at various pH values and salt concentrations are discussed and than one type of interaction mechanism is operational (12the binding isotherm is reported. The binding and thermodynamic data obtained in this study can provide information on the mecha-15). Among the factors deemed influential in the interaction nism and process of imidazole and protein binding with immobiinclude the number of electron-donating groups on the prolized metal ions.