Isolation and amino acid composition of insoluble elastin bovine foetal and adult aorta and ligamentum nuchae

Abstract

Insoluble elastin has been prepared from bovine foetal and adult aorta and ligamentum nuchae by a combination of enzymic digestion which avoid the use of hot alkali treatment conventionally employed in the isolation of elastin. Treatment of the homogenised tissue with crude bacterial α-amylase enabled most of the collagen to be extracted as a dispersion in dilute acetic acid. The residual collagen associated with the insoluble elastin was removed by digestion with collagenase. The amino acid composition of these enzyme prepared elastins and the corresponding hot alkali insoluble elastins were compared. The enzyme prepared elastins contained slightly more hydrophilic amino acid residues than the alkali insoluble elastins. The enzyme prepared elastins are more suitable than the hot alkali prepared elastins for a chemical study of the interchain cross-linkages present in tissue elastin in its naturally occurring physiologic state.