Abstract

AbstractA CD study was carried out on elastin peptide samples obtained from porcine and normal and pathological human aortas. Different solubilization procedures were used: (1) an ethanolic‐KOH hydrolysis to obtain porcine κ‐elastins; (2) oxalic acid hydrolysis to obtain porcine α‐ and β‐elastins; and (3) enzymatic digestions and a partial acid hydrolysis to obtain porcine and human crosslinked peptides. The comparison of the results obtained from the dichroic study of porcine and normal human aorta peptides does not reveal any differences. On the contrary, the dichroic spectra obtained for the human pathological aorta peptides at different stages of atheromateous lesions exhibit some differences which are attributed to some variations of the conformation around the bridging zones.

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