Divalent metal cation binding properties of human prothymosin α

• DOI: 10.1046/j.1432-1327.2000.01529.x
• Publication Date: 2003-03-11T17:50:33Z
• Authors: Nina V. Chichkova; Alexandra G. Evst...; Ilya G. Lyakhov; Andrey S. Tsvetkov; Tatyana A. Smirnova; Ruben N. Karapetian; Elena M. Karger; Andrey B. Vartape...
• Keywords: Divalent

The divalent cation binding properties of human prothymosin α, an abundant nuclear protein involved in cell proliferation, were evaluated. By using α retardation on a weak chelating resin charged with various cations, specific Zn 2+ ions by was observed. This finding further confirmed the equilibrium dialysis analysis which demonstrated that, within micromolar range concentrations, could bind up to three zinc presence 100 m NaCl and 13 absence NaCl. Equilibrium also revealed that Ca , although parameters less pronounced than those terms number metal bound, K D values, resistance bound effects interaction its putative partners, Rev HIV type 1 histone H1, examined. We binds but not H1 significantly enhanced calcium ions. Our data suggest modes are distinct observed calcium‐binding might be functionally relevant.