International journal of radiation biology and related studies in physics, chemistry, and medicine 1984-03-01

Enzymatic digestibility of peptides cross-linked by ionizing radiation.

M Dizdaroglu, E Gajewski, M G Simic

Index: Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 45(3) , 283-95, (1984)

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Abstract

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.

Related Compounds

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H-Phe-Phe-OH Structure H-Phe-Phe-OH
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