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Purification, biochemical, and structural characterization of a novel fibrinolytic enzyme from Mucor subtilissimus UCP 1262.

Bioprocess and biosystems engineering (2017-05-14)
Thiago Pajeú Nascimento, Amanda Emmanuelle Sales, Tatiana Souza Porto, Romero Marcos Pedrosa Brandão Costa, Leonid Breydo, Vladimir N Uversky, Ana Lúcia Figueiredo Porto, Attilio Converti
RESUMEN

Fibrinolytic proteases are enzymes that degrade fibrin. They provide a promising alternative to existing drugs for thrombolytic therapy. A protease isolated from the filamentous fungus Mucor subtilissimus UCP 1262 was purified in three steps by ammonium sulfate fractionation, ion exchange, and molecular exclusion chromatographies, and characterized biochemically and structurally. The purified protease exhibited a molecular mass of 20 kDa, an apparent isoelectric point of 4.94 and a secondary structure composed mainly of α-helices. Selectivity for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrate suggests that this enzyme is a chymotrypsin-like serine protease, whose activity was enhanced by the addition of Cu

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Sigma-Aldrich
Fibrinógeno from bovine plasma, Type I-S, 65-85% protein (≥75% of protein is clottable)