Further evidence for an active site polypeptide of galactosyl transferase.

In a previous report it was shown that galactosyl transferase activity after blotting from acrylamide gel was present in a molecular weight range of less than 14 kDa, in Triton X-100 (1). Molecular sieve chromatography on Superose 12, in the presence of Triton X-100, gave the same result. The low molecular weight activity peak was eluted together with peptides as a part of the covalent structure of the enzyme or as absolutely requires effectors. Peptide mapping showed a new poly-lysine-like peptide and a new hydrophobic peptide in this low molecular weight activity peak as effectors of the enzyme inside its hydrophobic environment.