Intrinsic enzyme activity associated with tropoelastin

Robert P. Mecham, Judith Ann Foster, Carl Franzblau

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

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
Volume446
Issue number1
DOIs
StatePublished - Sep 28 1976
Externally publishedYes

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