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(Na + + K + )‐ATPase: Function, structure, and conformations
Author(s) -
Stahl William L.
Publication year - 1984
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410160718
Subject(s) - enzyme , adenosine triphosphatase , extracellular , atpase , homeostasis , mechanism (biology) , chemistry , function (biology) , microbiology and biotechnology , biophysics , biochemistry , triphosphatase , biology , physics , quantum mechanics
Na + ‐ and K + ‐dependent adenosine triphosphatase [(Na + + K + )‐ATPase] plays a pivotal role in the homeostasis of Na + , K + , and Ca 2+ in cells. Although the structural and enzymatic characteristics of this enzyme are being rapidly elucidated, the mechanisms underlying the vectorial movement of ions remain unclear. An understanding of the mechanism and localization of this enzyme is of importance in the study of epilepsy, since a possible defect leading to epilepsy may involve the inability of cellular elements to clear extracellular K + . Studies of conformational changes associated with the binding of specific ligands to the enzyme are being used to understand better the mechanism of the (Na + + K + )‐ATPase found in nervous tissue and transporting epithelia.