Biochemistry (Moscow)

, Volume 67, Issue 4, pp 503–509

Interaction between Tubulin and Na2+,K2+-ATPase in Brain Stem Neurons

  • N. M. Vladimirova
  • E. N. Sautkina
  • T. V. Ovchinnikova
  • N. A. Potapenko
Article

DOI: 10.1023/A:1015202610797

Cite this article as:
Vladimirova, N.M., Sautkina, E.N., Ovchinnikova, T.V. et al. Biochemistry (Moscow) (2002) 67: 503. doi:10.1023/A:1015202610797

Abstract

Functionally active Na2+,K2+-ATPase isozymes containing three types of the catalytic subunits (α1, α2, and α3) were obtained from calf brain by two methods: selective removal of contaminating proteins according to Jorgensen (1974) and selective solubilization of the enzyme with subsequent reformation of the membrane structure according to Esmann (1988). All preparations were characterized with respect to ouabain-inhibition constants. The presence of the cytoskeleton protein tubulin (β3 isoform) in the high-molecular-weight complex of Na2+,K2+-ATPase α3β1 isozyme from brain stem axolemma and the junction between Na2+,K2+-ATPase α3 subunit and tubulin β3 subunit are shown for the first time.

Na2+,K2+-ATPase isoforms isozymes axolemma tubulin 

Copyright information

© MAIK “Nauka/Interperiodica” 2002

Authors and Affiliations

  • N. M. Vladimirova
    • 1
  • E. N. Sautkina
    • 1
  • T. V. Ovchinnikova
    • 1
  • N. A. Potapenko
    • 1
  1. 1.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia