The properties of slightly soluble Zn(II)-protein complexes in the form of a suspension

The properties of slightly soluble Zn(II)-protein complexes in the form of a suspension. Slightly soluble Zn(II) complexes with selected hormones were obtained in the form of a suspension. Zn(II)-protein complexes were obtained at different ligand concentrations. The amount of Zn(II) in μM bound to a protein increases along with an increase in the added ligand concentration. This amount is statistically significant as far as its binding to INS is concerned. Proteins bind to Zn(II) through two classes of binding sites (n). Most Zn(II) binds to albumin and least to LH and FSH. The protein molecular weight and number of its amino acid residues have an influence on binding Zn(II) to a selected protein. Zn(II) has the highest affinity for PRL and INS, and the lowest for albumin and FSH. The kinetics analysis of Zn(II) binding to proteins has shown that Zn(II) creates the most stable complexes with PRL, INS, and LH. Relatively, weak complexes were obtained with albumin and FSH. The protein molecular weight and the number of its amino acid residues have a significant influence on the stability of Zn(II)-protein complex. The lower protein molecular weight and number of its amino acid residues, the more stable Zn(II)-protein complex is. The stability of complexes is also associated with the amount of Zn(II) bound to a protein and its affinity for a protein.