Synthesis of Peptides by Bovine Gastricsin

Bovine gastricsin catalyzes peptide synthesis over an optimum range of pH 4~5, resulting in satisfactory yields of methyl esters and p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino acid residues form new peptide bonds. The effectiveness of the enzyme also depends on the nature of adjacent amino acid residues. An aspartic proteinase with a characteristic gastricsin specificity pattern would be useful for the synthesis of middle-length peptides.