Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1945868 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2007 | 6 Pages |
Recently, two novel mammalian aquaporins (AQPs), AQPs 11 and 12, have been identified and classified as members of a new AQP subfamily, the “subcellular AQPs”. In members of this subfamily one of the two asparagine–proline–alanine (NPA) motifs, which play a crucial role in selective water conduction, are not completely conserved. Mouse AQP11 (mAQP11) was expressed in Sf9 cells and purified using the detergent Fos-choline 10. The protein was reconstituted into liposomes, which were used for water conduction studies with a stopped-flow device. Single water permeability (pf) of AQP11 was measured to be 1.72 ± 0.03 × 10− 13 cm3/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels.