Abstract
Elastin was isolated and purified by a procedure which sequentially removed lipids, collagen, structural glycoproteins and the microfibrillar proteins. Crosslinking profiles were obtained by column chromatography either after reduction with 3[H]NaBH4 or after reaction with 14[C]NaCN and NH3. Examination of the crosslinking profiles of the elastins from various tissue regions revealed differences in the type, distribution and quality of crosslinks.
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