αβ protomers of Na+,K+-ATPase from microsomes of duck salt gland are mostly monomeric: Formation of higher oligomers does not modify molecular activity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 7, 2000, Pages 3195-3200

  Martin, Dwight W ^a   Marecek, James ^a   Scarlata, Suzanne ^a   Sachs, John R ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5 CARBOXYFLUORESCEIN 6 AMINOHEXYL OUABAIN; 6 CARBOXYFLUORESCEIN 6 AMINOHEXYL OUABAIN; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANTHROYLOUABAIN; F ACTIN; MONOMER; N (7 NITROBENZ 2 OXA 1,3 DIAZOL 4 YL) 6 AMINOHEXYL OUABAIN; OLIGOMER; OUABAIN; PHALLOIDIN; UNCLASSIFIED DRUG; 4 NITROPHENYLPHOSPHATASE; BIOPOLYMER;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CYTOSKELETON; DUCK; ENERGY TRANSFER; ENZYME MECHANISM; FLUORESCENCE; MICROSOME; NONHUMAN; PRIORITY JOURNAL; SALT GLAND; ANIMAL; CHEMISTRY; ELECTRON MICROSCOPY; ENZYMOLOGY; METABOLISM; PHOSPHORYLATION; ULTRASTRUCTURE;

ANAS SP.; ANIMALIA; STROPHANTHUS GRATUS;

4-NITROPHENYLPHOSPHATASE; ANIMALS; BIOPOLYMERS; DUCKS; MICROSCOPY, ELECTRON; MICROSOMES; NA(+)-K(+)-EXCHANGING ATPASE; PHOSPHORYLATION; SALT GLAND;

EID: 0034724091     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.050558397     Document Type: Article

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