Further characterization of the N-terminal copper(II)- and nickel(II)-binding motif of proteins. Studies of metal binding to chicken serum albumin and the native sequence peptide.

摘要: We have investigated the Cu(II)- and Ni(II)-binding properties of chicken serum albumin (CSA) native sequence tripeptide derived from N-terminus this protein. Spectrophotometric equilibrium dialysis experiments demonstrate that Cu(II) Ni(II) bind non-specifically at CSA. Proton displacement studies show histidine residue in fourth position protein does not appear to participate binding two metals. Consistent results were obtained with L-aspartyl-L-alanyl-L-glutamic acid N-methylamide. The presented here neither glutamic third nor It is known, however, a number other albumins possess high-affinity sites. Our provide further evidence N-terminal Cu(II)/Ni(II)-binding motif requires order specifically.