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dc.date.accessioned 2022-12-07T13:38:59Z
dc.date.available 2022-12-07T13:38:59Z
dc.date.issued 2006-05
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/146979
dc.description.abstract We overview the critical steps leading to the demonstration that each ~28 kD protein monomer of the water channel (or pore)¹ pierce the lipid bilayer part of the cell membrane allowing the passage of ~ 10¹³ water molecules per second. The biophysical approach gives a functional and physical image of the water pore close to what has recently been obtained from the amino acid sequence, crystallography and other advances from the cloning era of trans-membrane water transport. Paracellular “wide” water channels of some leaky epithelia are not covered here [cf. Whittembury and Reuss, 1992; Whittembury and Hill, 2000]. en
dc.language en es
dc.subject Fisiología es
dc.subject Aquaporin es
dc.subject Water channels es
dc.subject Cell membrane es
dc.title The old water channels are aquaporin proteins through which single files of water molecules cross cell membranes en
dc.type Articulo es
sedici.identifier.uri https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n10_may.pdf es
sedici.identifier.issn 1669-5410 es
sedici.creator.person Gutiérrez, Antonio M. es
sedici.creator.person Echevarría, Miriam es
sedici.creator.person Whittembury, Guillermo es
sedici.subject.materias Ciencias Médicas es
sedici.description.fulltext true es
mods.originInfo.place Sociedad Argentina de Fisiología es
sedici.subtype Revision es
sedici.rights.license Creative Commons Attribution 4.0 International (CC BY 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Physiological Mini Reviews (PMR) es
sedici.relation.journalVolumeAndIssue vol. 1, no. 10 es


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Creative Commons Attribution 4.0 International (CC BY 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution 4.0 International (CC BY 4.0)