alanyl-alanyl-alanyl-alanine and phenylalanyl-phenylalanyl-phenylalanine

p6gestibility by proteolytic enzymes of peptides cross-linked by ionizing radiation was investigated. Small peptides of alanine and phenylalanine were chosen as model compounds and aminopeptidases and carboxypeptidases were used as proteolytic enzymes. Peptides exposed to gamma-radiation in aqueous solution were analysed by high-performance liquid chromatography before and after hydrolysis by aminopeptidase M, leucine aminopeptidase, carboxypeptidase A and carboxypeptidase Y. The results obtained clearly demonstrate the different actions of these enzymes on cross-linked aliphatic and aromatic peptides. Peptide bonds of cross-linked dipeptides of alanine were completely resistant to enzymatic hydrolysis whereas the enzymes, except for carboxypeptidase Y, cleaved all peptide bonds of cross-linked peptides of phenylalanine. The actions of the enzymes on these particular compounds are discussed in detail.

Topics: Aminopeptidases; Carboxypeptidases; Carboxypeptidases A; CD13 Antigens; Chromatography, High Pressure Liquid; Cobalt Radioisotopes; Dipeptides; Gamma Rays; Leucyl Aminopeptidase; Oligopeptides; Peptide Hydrolases; Peptides