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

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

• Publisher: Elsevier Science
• Year: 1997
• Tongue: English
• Weight: 105 KB
• Volume: 190
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1997.4814

✦ Synopsis

viewed by Wong (8), and the interaction behavior of immo-In this investigation, employing a highly sensitive microcalorimbilized metal ions in PEG liquid phases and in solid phases eter, we measure the influence of pH value and salt concentration with proteins have been systematically explored in previous on the heat of interaction between lysozyme and CS-IDA-Cu(II) literatures (9, 10). In general, protein surface topography gel. The direct enthalpy measurement of the interaction provides and the chemical and physical nature of the interaction conthermodynamic information regarding the binding behavior of lyditions affect how protein interacts with immobilized metal sozyme toward the immobilized metal ion. The binding enthalpy ions. The coordination compound, which is formed by the altered by adsorbed lysozyme at various pH values and salt concenaccessible electron-donating group on the protein's surface trations are measured. The findings, along with the reported bind-

and the immobilized metal ion, is the major binding interacing isotherm, are discussed herein.