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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: kakinuma y. J Biochem. 1999 Feb;125(2):414-21. doi: 10.1093/oxfordjournals.jbchem.a022302. J Biochem. 1999. PMID: 9990142 Free article.
This amount is 500-fold larger than that reported in the previous paper [Murata, T., Takase, K., Yamato, I., Igarashi, K., and Kakinuma, Y. (1997) J. Biol. Chem. 272, 24885-24890]. The purified enzyme shows a high specific activity of ATP hydrolysis (35.7 micromol P …
This amount is 500-fold larger than that reported in the previous paper [Murata, T., Takase, K., Yamato, I., Igarashi, K., and Kakinuma …
ATP-dependent affinity change of Na+-binding sites of V-ATPase.
Murata T, Kakinuma Y, Yamato I. Murata T, et al. Among authors: kakinuma y. J Biol Chem. 2001 Dec 21;276(51):48337-40. doi: 10.1074/jbc.M106821200. Epub 2001 Sep 13. J Biol Chem. 2001. PMID: 11557766 Free article.
V-type Na(+)-ATPase of Enterococcus hirae binds about six (6 +/- 1) Na(+) ions/enzyme molecule with a high affinity (Murata, T., Igarashi, K., Kakinuma, Y., and Yamato, I. (2000) J. Biol. Chem. 275, 13415-13419). ...
V-type Na(+)-ATPase of Enterococcus hirae binds about six (6 +/- 1) Na(+) ions/enzyme molecule with a high affinity (Murata, T., Igarashi, K …
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: kakinuma y. 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). ...
We have reported previously on ATP-dependent negative cooperativity for Na+ coupling of this enzyme (Murata, T., Kakinuma, Y., …
284 results