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Activation energy and phospholipid requirements of membrane-bound adenosine triphosphatases

โœ Scribed by J.S. Charnock; D.A. Cook; A.F. Almeida; Rebecca To


Book ID
115701829
Publisher
Elsevier Science
Year
1973
Tongue
English
Weight
606 KB
Volume
159
Category
Article
ISSN
0003-9861

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EPR and water proton relaxation rate ( ] / T i ) studies of partially (40%) and "fully" (90%) purified preparations of membrane-bound (Na' + K+) activated ATPase from sheep kidney indicate one tight binding site for Mn" per enzyme dimer, with a dissociation constant (K,, = 0.88 pM) in agreement with