title: Binding of zinc and cadmium to human serum albumin.
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.
authors.affiliation: Institut für Anorganische und Analytische Chemie, Universität Innsbruck, Osterreich.
authors.forename: S T
authors.initials: ST
authors.lastname: Trisak
authors.forename: P
authors.initials: P
authors.lastname: Doumgdee
authors.forename: B M
authors.initials: BM
authors.lastname: Rode
mesh_terms: D002104:Cadmium / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011199:Potentiometry; D011485:Protein Binding; D011522:Protons; D012709:Serum Albumin / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
chemical_list: D011522:Protons; D012709:Serum Albumin; D002104:Cadmium; D006639:Histidine; D015032:Zinc