| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5163928 | Phytochemistry | 2017 | 23 Pages |
Abstract
Eight cysteine peptidases were isolated from A. comosus stems, including a novel protease, by covalent grafting of a specific and reversible thiol-pegylation reagent. Mass spectroscopy and Far-UV CD analyses revealed very close molecular masses and secondary structure contents. Enzymatic activity measurements using different Fluorophore and chromophore substrates as well as protein substrates clearly demonstrated different substate specificities and allowed to clearly distinguish three different proteases populations.135
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Authors
André Matagne, Laetitia Bolle, Rachida El Mahyaoui, Danielle Baeyens-Volant, Mohamed Azarkan,