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Intrinsic enzyme activity associated with tropoelastin.

R P Mecham·J A Foster·C Franzblau
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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 degrees C) and can be inhibited by disodium ethylenediaminetetraacetate, N-ethylmaleimide, sulfite, soybean trypsin inhibitor and human alpha-1-antitrypsin. The fragmentation pattern appears to be specific and reproducible.

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Amino AcidsAnimalsAortaChickensEdetic AcidElastinElectrophoresis, Polyacrylamide GelEthylmaleimideHumansLathyrismMolecular WeightPeptide HydrolasesSulfidesSulfitesTropoelastinTrypsin Inhibitor, Bowman-Birk Soybeanalpha 1-AntitrypsinJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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R P Mecham, J A Foster, C Franzblau. 1976-09-28. Intrinsic enzyme activity associated with tropoelastin.. https://doi.org/10.1016/0005-2795(76)90115-x

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