These authors equally contributed to this work.
A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii
Article first published online: 10 DEC 2013
© 2013 FEBS
Volume 281, Issue 1, pages 401–415, January 2014
How to Cite
Gogliettino, M., Riccio, A., Balestrieri, M., Cocca, E., Facchiano, A., D'Arco, T. M., Tesoro, C., Rossi, M. and Palmieri, G. (2014), A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii. FEBS Journal, 281: 401–415. doi: 10.1111/febs.12610
- Issue published online: 2 JAN 2014
- Article first published online: 10 DEC 2013
- Accepted manuscript online: 9 NOV 2013 10:13AM EST
- Manuscript Accepted: 5 NOV 2013
- Manuscript Revised: 11 OCT 2013
- Manuscript Received: 26 JUL 2013
- Italian MIUR
- CNR organizations
Table S1. APEH chains utilized for phylogenetic analysis.
Table S2A. Purification of APEH-2Tb from RBCs of the notothenioid fish Trematomus bernacchii.
Table S2B. Purification of APEH-1Tb from liver of the notothenioid fish T. bernacchii.
Table S3. List of charged residues found within an increasing distance from the three amino acids of the catalytic triad.
Fig. S1. cDNA sequence of apeh-1Tb and apeh-2Tb from T. bernacchii with the deduced amino acid sequences.
Fig. S2. Muscle alignment of APEH-1Tb and APEH-2Tb sequences with those of APEHs from different sources.
Fig. S3. Gel filtration chromatography on a Superdex 200 column of APEH-2Tb from T. bernacchii.
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.