Binding of zinc and cadmium to human serum albumin |
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| Authors: | S T Trisak P Doumgdee B M Rode |
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| Affiliation: | 1. Chemistry Department, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia;2. Chemistry Department, University College in Al–Jamoum, Umm Al-Qura University, Makkah 21955, Saudi Arabia;3. Chemistry Department, Faculty of Science, Damietta University, Damietta 34517, Egypt;4. Department of Chemistry, Faculty of Science, Taif University, P.O. BOX 7685, Taif 21944, Saudi Arabia;1. College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, PR China;2. Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou 225009, PR China;1. Department of Chemistry, Faculty of Applied Science, Umm AL-Qura University, P.O. Box 16722, Makkah 21955, Saudi Arabia;2. Department of Chemistry, Faculty of Science, King Abdulaziz University, P. O. Box 80203, Jeddah 21589, Saudi Arabia |
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| Abstract: | 1. The interaction of zinc and cadmium ion with human serum albumin (HSA) is evaluated and compared by potentiometric titration method and computer simulation of complex equilibria. 2. Zinc binds to histidine and free amino groups, cadmium in addition to basic functional groups of the protein. 3. Whereas zinc binds stronger in 1:1 complexes, chelate binding favours cadmium ions. 4. Within biological pH-conditions, high amounts Zn(II) and even more of Cd(II) will be bound to HSA. |
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