Smeets P, Granger M, Van Nispen J W, Bloemendal H, Tesser G I
Int J Pept Protein Res. 1977 Jan;9(1):52-6.
Application of the 2-methylsulfonylethyloxycarbonyl group for temporary amino protection enables the synthesis from one precursor of des-Nalpha1-acetyl-alpha-MSH, the two mono N-acetylated forms (in positions I and II) and the diacetyl form of this tridecapeptide amideq The free tridecapeptide amide, although structurally unrelated to the normal substrate, was recognized by an enzyme occurring in calf eye-lens tissue. The product of the enzymatic reaction was exclusively alpha-MSH. Partial sequences derived from the N-terminus were less rapidly acetylated or not at all, depending on their chain length. The enzyme, therefore, appears to direct its activity to free N-terminal alpha-amino groups of peptides exceeding a certain critical chain length. Acetylation of epsilon-amino functions did not occur.
