Digestion of elastin by porcine pancreatic elastase I and elastase II

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Abstract
Elastin was fully solubilized by digestion with elastase I or elastase II. Each digest was separated into high-MW and low MW fractions that were characterized by the correspondence to their amino acid content, N-terminal sequence and C-terminal amino acids. Although the relative amount of amino acids in the low-MW fraction obtained by digestion with elastase I was lower than in digestion with elastase II, no major difference in the type of bonds cleaved in the low- or high-MW fractions of each digest were seen. There was a remarkable difference in the ype of bond cleaved by the 2 enzymes. While elastase I cleaved mostly Ala-Ala and also Ala-Gly bonds, elastase II hydrolyzed Leu-Ala, Leu-Gly, Phe-Ala, Phe-Gly, Tyr-Ala and Tyr-Gly bonds. Theoretical calculations suggested that digests were composed of cross-linked peptides that vary not only in the molecular size but also in the number of crosslinks found in peptides of the same size.