Copper(II)-binding ability of human alpha-fetoprotein.

摘要: The copper(II)-binding ability of human α-fetoproteins, which were purified from umbilical cord serum and ascites fluid a hepatoma-bearing patient, was examined by equilibrium dialysis gel filtration methods. pH dependence the α-fetoprotein quite similar to that albumin. α-Fetoprotein bound 1 mol copper(II) ion per protein above 6.0 0.5 at 5.4, is close pK value imidazole group histidine. Photooxidation in presence methylene blue resulted loss parallel with destruction histidyl residues. A synthetic amino-terminal undecapeptide also ion. These results indicate residue aminoterminal region plays an important role protein.