Title : Evidence for a glycerol pathway through aquaporin 1 (CHIP28) channels.

Pub. Date : 1995 Jul

PMID : 7491270






4 Functional Relationships(s)
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1 Permeabilities to glycerol and small non-electrolytes of three Aquaporin 1 CHIP (AQP1) water channels were measured in AQP1 cRNA-injected Xenopus laevis oocytes and in human AQP1 channels reconstituted in proteoliposomes. Water aquaporin 1 (Colton blood group) L homeolog Xenopus laevis
2 Permeabilities to glycerol and small non-electrolytes of three Aquaporin 1 CHIP (AQP1) water channels were measured in AQP1 cRNA-injected Xenopus laevis oocytes and in human AQP1 channels reconstituted in proteoliposomes. Water aquaporin 1 (Colton blood group) L homeolog Xenopus laevis
3 Permeabilities to glycerol and small non-electrolytes of three Aquaporin 1 CHIP (AQP1) water channels were measured in AQP1 cRNA-injected Xenopus laevis oocytes and in human AQP1 channels reconstituted in proteoliposomes. Water aquaporin 1 (Colton blood group) L homeolog Xenopus laevis
4 All these results provide strong evidence that water and certain small solutes permeate the AQP1 channels expressed at the surface of X. laevis oocytes or reconstituted in proteoliposomes. Water aquaporin 1 (Colton blood group) L homeolog Xenopus laevis