Two CNBr fragments of sea whale prolactin containing 69 and 41 amino acid residues, respectively, were hydrolyzed by trypsin, and the hydrolytic products were separated by the paper peptide mapping technique. The amino acid sequence of 17 homogeneous peptides was studied by the Edman method as well as by hydrolysis with carboxypeptidases A and B. Based on the experimental data and the previously published results the primary structure of sea whale prolactin made up of 199 amino acid residues was proposed.
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