๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Interactions of Imidazole and Proteins with Immobilized Cu(II) Ions: Effects of Structure, Salt Concentration, and pH in Affinity and Binding Capacity

โœ Scribed by Wen-Yih Chen; Ching-Fa Wu; Chih-Chung Liu


Publisher
Elsevier Science
Year
1996
Tongue
English
Weight
168 KB
Volume
180
Category
Article
ISSN
0021-9797

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Microcalorimetric Studies of the Interac
โœ Ching-Fa Wu; Wen-Yih Chen; Jiunn-Fwu Lee ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 116 KB

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 pr

Microcalorimetric Studies of the Interac
โœ Wen-Yih Chen; Jiunn-Fwu Lee; Ching-Fa Wu; Heng-Kwong Tsao ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 105 KB

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 pr

Microcalorimetric Studies of the Interac
โœ Fu-Yung Lin; Wen-Yih Chen; Lung-Ching Sang ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 91 KB

This study extends previous research on the interaction of biomaterials with immobilized Cu(II) by isothermal titration calorimetry (ITC) on Fe(III). The difference of the binding behavior of protein with that of the immobilized metal ions is also discussed. For the immobilized Fe(III), ITC results