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Na + transport by reconstituted Na + ,K + ‐ATPase in the presence of various nucleotides
Author(s) -
Svinukhova Irina A.,
Boldyrev Alexander A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80082-0
Subject(s) - nucleotide , chemistry , gtp' , atpase , proton , ouabain , substrate (aquarium) , enzyme , sodium , biochemistry , physics , biology , ecology , organic chemistry , quantum mechanics , gene
The ability of ATP, CTP, ITP, GTP, UTP and two synthetic ATP analogs to provide for ouabain‐sensitive Na + accumulation into proteoliposomes with a reconstituted Na + ,K + ‐ATPase (ATP phosphohydrolase, EC 3.6.1.37) was investigated. A correlation between the proton‐accepting properties of the nucleotides and their ability to provide for active transport was found. The proton‐accepting properties of the substrate seem to be a necessary condition for the shift from the K‐form to Na form of Na + ,K + ‐ ATPase — an immutable step in the active translocation of Na + and K + through the Na + pump.