In this paper have been studied properties of a product that arose from the interaction of malonaldehyde with collagen. It has been shown by an amino acid analysis that malonaldehyde reacts in a significant way on lysine and tyrosine residues. The partcipation of tyrosine in the reaction with malonaldehyde has been further demonstrated by means of spectrophotometry. It has also been found that the hydrolysis by pronase is considerably modified with the cross linked collagen.
The amino acid sequences were determined of three peptide fragments, isolated from a pronase digest of collagen modified by malonaldehyde. The hypothesis was confirmed that lysine, and not tyrosine residues, participate in the formation of crosslinkages.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.