| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5165307 | Phytochemistry | 2012 | 12 Pages |
Abstract
⺠cDNA encoding an aspartic protease precursor was isolated from Cirsium vulgare flowers. ⺠The encoded protease (cirsin) shares with cyprosin a striking sequence similarity. ⺠Recombinant procirsin was active without undergoing any activation process. ⺠This precursor form displayed the typical proteolytic properties of aspartic proteases. ⺠Recombinant procirsin also cleaved κ-casein and displayed milk-clotting activity.
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Organic Chemistry
Authors
Daniela Lufrano, Rosário Faro, Pedro Castanheira, Gustavo Parisi, Paula VerÃssimo, Sandra Vairo-Cavalli, Isaura Simões, Carlos Faro,