Abstract
Rather drastic methods are commoly used to isolate elastic fibers from tissues; heating the tissue in 0.1 N NaOH (Lowry et. at., 1941) or autoclaving in water (Partridge, Davis and Adair, 1955) or dilute organic acid (Hall 1955) leaves a residue which is called elastin. As the name implies, the product so isolated undoubtedly represents partially degraded elastic fibers. In an attempt to isolate elastic fibers in a form more closely resembling that of the native state we have used digestion by trypsin and collagenase to remove extraneous protein. This report shows the difference in amino acid composition between elastin prepared by this procedure and that prepared by heating lung connective tissue in 0.1 N NaOH.
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