ABSTRACT
In 1949, a report on "state-of-the-art" chemical synthesis of peptides was presented by J. S. Fruton. On this occasion the author also pointed out the possibility of applying proteases to preparative scale peptide synthesis. Peptide bond formation by means of immobilized trypsin was studied by Konnecke et al. Evidently, the interest in protease-catalyzed peptide syntheses markedly waned as the current concept of ribosome mediated protein biosynthesis developed. Papain was the very first protease whose proteosynthetic capacity was exploited for the preparation of a well-defined peptide. Pepsin, a protease found in the gastric juice, is the best-known member of the family of the so-called "acid proteases". Fruton's previous suggestion concerning protease-controlled peptide synthesis was only taken up in the late 1970s when the Japanese groups of Isowa and Morihara initiated their pioneering studies on the ability of a series of proteases to act as catalysts in peptide synthetic chemistry.
