| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1975132 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2015 | 8 Pages |
Aldehyde dehydrogenases (ALDHs), which oxidize aldehyde to corresponding acids, play a major role in the detoxification of various endogenous and exogenous aldehydes. In this study, we cloned and characterized ALDH9 (designated LjALDH9) from Arctic lamprey Lampetra japonica. The open reading frame of LjALDH9 was 1566 bp, encoding 521 amino acids with a predicted molecular mass of 55.68 kDa. LjALDH9 protein had a signal peptide and Aldedh domain with the active site Cys315. In addition, LjALDH9 shares high sequence homology with ALDH9 of jawed vertebrates. Real-time quantitative PCR revealed that LjALDH9 was highly expressed in the buccal gland. A reactive LjALDH9 protein was obtained by prokaryotic expression, two-step-denaturing and refolding and affinity purification. During enzyme activity analysis of recombinant LjALDH9, we found that the most suitable reaction conditions were pH 7.0, 16–23 °C and Mn2 + as the activator. Our study provides theoretical proof that LjALDH9 plays an important role in the parasitic life phase of lamprey.
