Biochemistry (Moscow)

, Volume 81, Issue 3, pp 249–254 | Cite as

Identification of a region of the polypeptide chain of Na,K-ATPase α-subunit interacting with 67-kDa melittin-like protein

  • Yu. V. Kamanina
  • E. A. Klimanova
  • E. A. Dergousova
  • I. Yu. Petrushanko
  • O. D. LopinaEmail author


It was shown earlier that a 67-kDa protein purified from mouse kidney using polyclonal antibodies against melittin (a peptide from bee venom) interacted with Na,K-ATPase from rabbit kidney. In this study, a 43-kDa proteolytic fragment of Na,K-ATPase α-subunit interacting with the 67-kDa melittin-like protein was found. The α-subunit was hydrolyzed by trypsin in the presence of 0.5 mM ouabain (E2-conformation of Na,K-ATPase). A proteolytic fragment interacting with the 67-kDa melittin-like protein that was identified by mass-spectrometry is a region of the cytoplasmic domain of Na,K-ATPase α-subunit located between amino acid residues 591 and 775. The fragment includes a conservative DPPRA motif that occurs in many P-type ATPases. It was shown earlier that this motif of H,K-ATPase from gastric mucosa binds to melittin. We suggest that namely this motif of P-type ATPases is able to interact with proteins containing melittin-like modules.

Key words

Na,K-ATPase melittin-like proteins protein—protein interactions 





enzyme-linked immunosorbent assay


phenylmethylsulfonyl fluoride


phosphate-buffered saline


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Copyright information

© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  • Yu. V. Kamanina
    • 1
    • 2
  • E. A. Klimanova
    • 1
    • 2
  • E. A. Dergousova
    • 1
    • 2
  • I. Yu. Petrushanko
    • 2
  • O. D. Lopina
    • 1
    Email author
  1. 1.Department of Biochemistry, School of BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Engelhardt Institute of Molecular BiologyRussian Academy of SciencesMoscowRussia

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