ArticleThe Journal of eukaryotic microbiology
An Atypical Aquaporin 1 Derived From Paramecium multimicronucleatum Functions as a Multifunctional Channel That Permeates Water, Glycerol, and Urea.
Article in The Journal of eukaryotic microbiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
Although it had been reported that the translation product of the functional aquaporin gene, aqp1, is localized to the contractile vacuole complex of Paramecium multimicronucleatum, the molecules that pass through this channel protein had not been identified. In the present study, we introduced and expressed this protein in Xenopus oocytes and identified the molecules that pass through this channel protein using a swelling assay. The aqp1 mRNA injected into Xenopus oocytes was found to be sufficiently expressed and functional within the oocytes. As a result, P. multimicronucleatum AQP1 (PmAQP1) allowed water to pass through at a relatively slow rate of approximately 50 × 10
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