Abstract

The isolation of a high molecular weight species (130-140,000 daltons) of soluble elastin from the aortas of lathyritic chicks is described. In comparison to chick tropoelastin, the higher molecular weight material possesses an increased amount of acidic and hydroxyl amino acids and in contrast to tropoelastin, contains histidine, methionine and cystine residues. This molecular weight species of soluble elastin is susceptible to proteolytic degradation and can be shown to readily breakdown to lower molecular weight components including tropoelastin.

Original languageEnglish
Pages (from-to)1399-1406
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume72
Issue number4
DOIs
StatePublished - Oct 18 1976

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