ABSTRACT
The concept of peptide synthesis by reversal of mass action in protease-catalyzed reactions dates back to 1898 when J. H. van't Hoff suggested that the protease "trypsin" might posses the inherent capacity to catalyze the synthesis of proteins from degradation products originally generated by its own proteolytic action. The possibility of the participation of hydrolases in not only the degradation but also the assembly of biological macromolecules was first suggested by the phenomenon of the so-called "reversible zymo-hydrolysis", by A. C. Hill to designate the maltase-catalyzed synthesis of maltose from glucose. In 1938, M. Bergmann and his collaborators were the first to describe the enzymatic synthesis of well-defined peptides. The idea of protein biosynthesis by "reversible enzymic hydrolysis" had for some time been considered to be confirmed by the phenomenon of the so-called "plastein-reaction". Plastein formation was observed upon addition of pepsin, papain, trypsin, and chymotrypsin to concentrated solutions of "peptic" partial-hydrolysates.
