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The Mechanistic Requirements Of Passive H+ Import Through The Na, K-Atpase, Kevin S. Stanley
The Mechanistic Requirements Of Passive H+ Import Through The Na, K-Atpase, Kevin S. Stanley
Theses and Dissertations
This work focuses on the elucidation of the mechanism of passive proton import through the Na,K-ATPase. This enzyme uses the energy in ATP hydrolysis to exchange three intracellular Na+ for two extracellular K+ to maintain ion gradients within the cell, and while in the absence of physiological external Na+ and K+, the phosphorylated externally open (E2P) conformation passively imports protons, generating an inward current (IH). Chapter one reports on the effects of intracellular cations and nucleotides to shift the Na,K-ATPase into the E2P conformation. We identified that a combination of either internal Na+ and ATP or K+ and Pi. In …
Altered Na, K- Atpase Isoform Expression In Artemia Franciscana In Response To Hypersaline Environments, Jessica Drenth
Altered Na, K- Atpase Isoform Expression In Artemia Franciscana In Response To Hypersaline Environments, Jessica Drenth
Theses and Dissertations
The Na,K-ATPase (NKA) is an essential membrane pump that helps to establish cell ion gradients, and regulate intracellular salt in many organisms. One such species, Artemia franciscana (brine shrimp), extreme halophiles which live in hypersaline environments, expresses 2 distinct α-catalytic subunits of the NKA. One of these subunits, α2-(KK), has two key lysine substitutions located within the cation binding sites. Prior work has demonstrated this specific subunit may be directly involved in brine shrimp adaptation to their extreme environments. However, the precise molecular and physiological effects of α2-(KK) have not been entirely elucidated. I determined through immunohistochemistry that my initial …