The functional unit of Na,K-ATPase is a monomeric αβ protomer

Biochemical and Biophysical Research Communications

Volumn 280, Issue 5, 2001, Pages 1364-1366

  Takeda, Kazuo ^a   Kawamura, Masaru ^a  

^a UNIVERSITY OF OCCUPATIONAL AND ENVIRONMENTAL HEALTH   (Japan)

Author keywords

Functional unit; Na,K ATPase; Oligomerization; Xenopus oocyte

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM); MONOMER; OUABAIN; RUBIDIUM;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; BETA CHAIN; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; MEMBRANE BINDING; NONHUMAN; OLIGOMERIZATION; OOCYTE; PRIORITY JOURNAL; PROMOTER REGION; XENOPUS;

STROPHANTHUS GRATUS;

EID: 0034815977     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.4292     Document Type: Article

References (12)

1. +-ATPase
2. +-ATPase is the αβ-protomer
3. +-ATPase
4. +-ATPase
5. +-ATPase
6. +-ATPase from microsomes of duck salt gland are mostly monomeric; Formation of higher oligomers does not modify molecular activity
7. Primary structure of the α-subunit of Torpedo californica (Na,K)ATPase deduced from cDNA sequence
8. +-ATPase
9. A possible role of the β-subunit of (Na,K)-ATPase in facilitating correct assembly of the α subunit into the membrane
10. An improved assay for nanomole amounts of inorganic phosphate
11. 3 Na,K-ATPase complexes