Abstract
Our recent paper concerning bovine trypsinogen 1,2 presented a description of the primary structure of this protein, including the disulfide bridges. However, at that time an unequivocal assignment of all amino acid residues had not been made for several amino acid residues (positions 121, 177, 180). Thus it was not known whether these residues occurred in the form of acids or amides. The aspartic acid residue in position 151 has now been correctly determined as asparagine. The aim of the present communication was to remove all these uncertainties and to complete the investigation of the covalent structure of this protein. A preliminary report of this work was presented at the Third Federation Meeting of European Biochemical Societies 3.
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