Interactions of malonaldehyde with collagen. IV. localisation of malonaldehyde binding site in collagen molecule.

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.

Interaction of malonaldehyde with collagen. III. Binding site characteristic of malonaldehyde with respect to collagen.

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.