Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10797971 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 13 Pages |
Abstract
âºThe human sodium/iodide symporter (NIS) has been purified for the first time. âºNIS protein exists mainly as a dimer that is stabilised by a disulfide bridge. âºA proteolytic C-terminal fragment of NIS is present in quantity in various species. âºCo-expression of C- and N-terminal fragments reconstitute a functional NIS.
Keywords
SECDDMHEPESDABHEKlithium dodecylsulfateIMACC12E8BCATRISMOPSLDSPAGE3,3′-diaminobenzidine4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid4-morpholinepropanesulfonic acidn-dodecyl β-d-maltoside4-morpholineethanesulfonic acidpolyacrylamide gel electrophoresisoctaethylene glycol monododecyl etherbicinchoninic acidTriton X100ThyroidOligomeric statesodium/iodide symporterhuman embryonic kidney cellscytomegalovirusCMVMeSpost-translational regulationMembrane proteinSize exclusion chromatographyimmobilized metal affinity chromatographyEukaryote
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Authors
Sylvaine Huc-Brandt, Didier Marcellin, Fanny Graslin, Olivier Averseng, Laurent Bellanger, Patrick Hivin, Eric Quemeneur, Cécile Basquin, Valérie Navarro, Thierry Pourcher, Elisabeth Darrouzet,