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)
Full Text: HTML
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
Related Articles:
2014-12-01
[Electrophoresis 35(23) , 3321-30, (2014)]
1984-01-30
[Life Sci. 34(5) , 427-36, (1984)]
2001-09-01
[Electrophoresis 22(15) , 3163-70, (2001)]
A symmetric inhibitor binds HIV-1 protease asymmetrically.
1993-01-26
[Biochemistry 32(3) , 937-47, (1993)]
2010-11-01
[FEBS J. 277(21) , 4549-61, (2010)]