The Amino‐Acid Sequences of Three Tryptic Glycopeptides from Human Ceruloplasmin

The isolation and amino‐acid and carbohydrate composition of three tryptic glycopeptides, containing 16,17 and 20 amino‐acid residues, respectively, from the neuraminidase‐treated major form of human ceruloplasmin have been described earlier. It has also been suggested that the peptides possibly represent all of the carbohydrate‐binding sites in the protein. The present paper describes the amino‐acid sequences of these peptides as obtained by stepwise Edman degradation and carboxypeptidase digestions of the whole peptides and their fragments after cleavage by chymotrypsin, pepsin and thermolysin. The results confirm that the carbohydrate in all cases is attached via an asparagine (or aspartic acid) residue, that is followed by an X‐Thr/Ser sequence. No sequence homologies are found when the peptides are compared to each other or to other glycopeptides of known sequence.