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Functional Analysis of the Disulfide Bonds of Na+/K+-ATPase β-subunit by Site-directed Mutagenesis

  • M. Kawamura
  • S. Noguchi
  • S. Ueno
  • M. Kusaba
  • K. Takeda

Abstract

The ion transporting Na+/K+-ATPase of animal plasma membranes consists of the catalytic α- and the glycosylated β-subunit All the functional roles in the catalytic activity of the enzyme so far known belong to the α-subunit, whereas those of the β-subunit remain still unknown. However, the β-subunit has been revealed to play important roles in the biogenesis of the enzyme. It acts as a stabilizer of the nascent α-subunit within the endoplasmic reticulum [9, 10] and takes part in targeting the resulting αβ -complex to the plasma membrane [2,12].

Keywords

ATPase Activity Disulfide Bond Xenopus Oocyte Transmembrane Segment Translation Product 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994

Authors and Affiliations

  • M. Kawamura
    • 2
  • S. Noguchi
    • 1
  • S. Ueno
    • 2
  • M. Kusaba
    • 1
  • K. Takeda
    • 2
  1. 1.Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems EngineeringKyushu Institute of TechnologyIizuka, 820Japan
  2. 2.Faculty of MedicineUniversity of Occupational and Environmental HealthKitakyushu, 807Japan

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