All the expected tryptic and CNBr peptides from bovine β‐casein A2 were previously isolated and analyzed [1]. The complete positioning of these peptides was reported later on [2].The present report deals with the sequencing of 65 amino acid residues at the carboxyl‐terminus of β‐casein A2: ‐His‐Gln‐Pro‐His‐Gln‐Pro‐Leu‐Pro‐Pro‐Thr‐Val‐Met‐Phe‐Pro‐Pro‐Gln‐Ser‐Val‐Leu‐ Ser‐Leu‐Ser‐Gln‐Ser‐Lys‐Val‐Leu‐Pro‐Val‐Pro‐Glu‐Lys‐Ala‐Val‐Pro‐Tyr‐Pro‐Gln‐Agr‐Asp‐Met‐Pro‐Ile‐Gln‐Ala‐Phe‐Leu‐Leu‐Tyr‐Gln‐Gln‐Pro‐Val‐Leu‐Gly‐Pro‐Val‐Arg‐Gly‐Pro‐Phe‐Pro‐Ile‐Ile‐Val · OH.This result was obtained by using well known methods such as enzymic or chemical cleavages of the peptide chain, fractionation of peptides by Sephadex or Dowex column chromatography, paper electrophoresis or chromatography, and sequential Edman degradation.The carboxyl‐terminal tryptic peptide is very likely identical with a peptide isolated by Matoba et al. [3] from a tryptic digest of whole casein, and characterized by its bitter taste.