The presence of an enzyme(s) associated with purified tropoelastin has been established. Results indicate that the enzyme(s) remains closely associated with the soluble elastin throughout the entire purification procedure suggesting that it is very tightly bound. Enzymatic activity is optimum through the pH range 7-9 (37 °C) and can be inhibited by disodium ethylenediaminetetraacetate, N-ethylmaleimide, sulfite, soybean trypsin inhibitor and human α-l-antitrypsin. The fragmentation pattern appears to be specific and reproducible.

Original languageEnglish
Pages (from-to)245-254
Number of pages10
JournalBBA - Protein Structure
Issue number1
StatePublished - Sep 28 1976


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