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Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation.
Kawano M, Igarashi K, Yamato I, Kakinuma Y. Kawano M, et al. Among authors: yamato i. J Biol Chem. 2002 Jul 5;277(27):24405-10. doi: 10.1074/jbc.M200973200. Epub 2002 Apr 30. J Biol Chem. 2002. PMID: 11983695 Free article.
We have reported previously on ATP-dependent negative cooperativity for Na+ coupling of this enzyme (Murata, T., Kakinuma, Y., and Yamato, I. (2001) J. Biol. Chem. 276, 48337-48340). The negative cooperativity for the Na+ dependence of ATPase activity was weakened b …
We have reported previously on ATP-dependent negative cooperativity for Na+ coupling of this enzyme (Murata, T., Kakinuma, Y., and Yamato …
Properties of the V0V1 Na+-ATPase from Enterococcus hirae and its V0 moiety.
Murata T, Takase K, Yamato I, Igarashi K, Kakinuma Y. Murata T, et al. Among authors: yamato i. J Biochem. 1999 Feb;125(2):414-21. doi: 10.1093/oxfordjournals.jbchem.a022302. J Biochem. 1999. PMID: 9990142 Free article.
We report here the large-scale purification of vacuolar (V0V1)-type Na+-ATPase from Enterococcus hirae achieved using column anion-exchange and gel filtration chromatographies; 32 mg of purified enzyme comprising nine subunits, A, B, C, D, E, F, G, I, and K, was obtained f …
We report here the large-scale purification of vacuolar (V0V1)-type Na+-ATPase from Enterococcus hirae achieved using column anion-exchange …
165 results