![]() ![]() Minimum enzyme unit for Na+/K+-ATPase is the αβ-protomer. Yutaro Hayashi, Kunihiro Mimura, Hideo Matsui, Toshio Takagi.Biochimica et Biophysica Acta (BBA) - Biomembranes 1990, 1029 Anomalies in the electrophoretic resolution of Na+/K+-ATPase catalytic subunit isoforms reveal unusual protein-detergent interactions. European Journal of Biochemistry 1991, 195 Phosphate binding and ATP-binding sites coexist in Na+/K+-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4. Biochemical and Biophysical Research Communications 1991, 174 Conformational transitions of detergent-solubilized Na,K-ATPase are conveniently monitored by the fluorescent probe 6-carboxy-eosin. Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes 1991, 1071 Kinetics of exchange reactions performed by reconstituted Na/K-ATPase. Functional reconstitution of the sodium pump. Journal of Biological Chemistry 1992, 267 ![]() Low affinity superphosphorylation of the Na,K-ATPase by ATP. One Phosphorylation Site per αβ-Protomer in Reconstituted Shark Na+/K+-ATPase. Purified Renal Na+/K+-ATPase Subunit Structure and Structure-Function Relationships of the N-Terminus of the α1- Subunit. Biochimica et Biophysica Acta (BBA) - Biomembranes 1995, 1235 Phosphorylation/dephosphorylation of reconstituted shark Na+,K+-ATPase: one phosphorylation site per αβ protomer. Biochimica et Biophysica Acta (BBA) - Biomembranes 1995, 1240 Quantification of the Na+/K+-pump in solubilized tissue by the ouabain binding method coupled with high-performance gel chromatography.
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