title: Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.
abstract: A histidine-rich fragment, Cp F5, with a molecular weight of 18,650 was isolated from human ceruloplasmin. It consists of 159 amino acids and contains a possible copper-binding site. The sequence of the first 18 NH2-terminal residues of Cp F5 was determined by automated Edman degradation. Cp F5 was cleaved by cyanogen bromide to produce nine fragments of from 2 to 63 residues. The amino acid sequence of all of the cyanogen bromide fragments was investigated using automated and manual Edman degradation, the fragments being digested with trypsin, chymotrypsin, thermolysin, staphylococcal protease, and pepsin as appropriate. The results, in conjunction with the data on the tryptic peptides reported in the accompanying paper (Kingston, I.B., Kingston, B.L., and Putnam, F.L. (1980) J. Biol. Chem. 255, 2886-2896), establish the complete amino acid sequence of Cp F5.
mesh_terms: D000595:Amino Acid Sequence; D002268:Carboxypeptidases; D002570:Ceruloplasmin; D003488:Cyanogen Bromide; D006639:Histidine / Q000032:analysis*; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases
chemical_list: D010446:Peptide Fragments; D006639:Histidine; D002570:Ceruloplasmin; D002268:Carboxypeptidases; D010447:Peptide Hydrolases; D003488:Cyanogen Bromide