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  Calorimetry of Na,K-ATPase

Stolz, M., Lewitzki, E., Schick, E., Mutz, M., Grell, E., & Lewitzki (2003). Calorimetry of Na,K-ATPase. Annals of the New York Academy of Sciences, 986(1), 245-246. doi:10.1111/j.1749-6632.2003.tb07172.x.

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 Creators:
Stolz, Michael1, Author           
Lewitzki, Erwin1, Author           
Schick, Eginhard1, Author           
Mutz, M.2, Author
Grell, Ernst1, Author           
Lewitzki, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Novartis Pharma AG, 4002 Basel, Switzerland, ou_persistent22              

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 Abstract: In order to characterize the overall subunit interaction and the thermal stability of purified Na,K-ATPase isolated from pig kidney and dogfish (Squalus acanthias) rectal gland,1 a differential scanning calorimetry (DSC) study is carried out (Fig. 1a). With regard to ligand binding, the interaction stoichiometry (number of active sites n per protomer) and the affinity of ouabain and nucleotide binding are investigated by titration calorimetry at 25°C. Similar to our earlier results,2 the DSC thermogram of the pig kidney enzyme shows a single, very narrow, and almost symmetric endothermic denaturation transition at 57.0°C and a full width at half-maximum of 3.5°C. This is indicative of a uniform denaturation process of high cooperativity involving all subunits. Our result differs markedly from a recent investigation and thus questions the relevance of the interpretation postulated therein.3 The thermogram of the dogfish enzyme shows a lower transition temperature (49.5°C) and a much broader transition range than for the kidney enzyme. In addition, it exhibits a well-separated pretransition at 37.5°C. The pretransition is tentatively_assigned to the γ-like subunit of the dogfish enzyme. The broader transition can be an expression of less ordered subunit associations. The transition temperature of the micellar dogfish enzyme (C12E8 solubilized) is 8°C lower than that of the membrane-bound state. This can be due to an increased water access of the protein in the micellar state. All overall ΔH values are around 18 MJ/mol.

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Language(s): eng - English
 Dates: 2003-04-01
 Publication Status: Published in print
 Pages: 2
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Annals of the New York Academy of Sciences
  Other : Ann. N.Y. Acad. Sci.
Source Genre: Journal
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Publ. Info: New York : New York Academy of Sciences
Pages: - Volume / Issue: 986 (1) Sequence Number: - Start / End Page: 245 - 246 Identifier: ISSN: 0077-8923
CoNE: https://pure.mpg.de/cone/journals/resource/954926958894_2