Steady-state kinetic analysis of the Na+/K+-ATPase. The effects of adenosine 5'-[beta, gamma-methylene] triphosphate on substrate kinetics.

scientific article

Steady-state kinetic analysis of the Na+/K+-ATPase. The effects of adenosine 5'-[beta, gamma-methylene] triphosphate on substrate kinetics. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/0005-2736(89)90085-0
P698PubMed publication ID19048683

P2093author name stringR C Rossi
P J Garrahan
P433issue1
P921main subjectadenosine triphosphateQ80863
P304page(s)85-94
P577publication date1989-05-01
P1433published inBiochimica et Biophysica ActaQ864239
P1476titleSteady-state kinetic analysis of the Na+/K+-ATPase. The effects of adenosine 5'-[beta, gamma-methylene] triphosphate on substrate kinetics.
P478volume981

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cites work (P2860)
Q67493731Actions of cadmium on basolateral plasma membrane proteins involved in calcium uptake by fish intestine
Q67913207Inhibition of the phosphatase activity of the red cell membrane Ca2+ pump by acidic phospholipids
Q43654792Low affinity superphosphorylation of the Na,K-ATPase by ATP
Q36412531Quaternary organic amines inhibit Na,K pump current in a voltage-dependent manner: direct evidence of an extracellular access channel in the Na,K-ATPase
Q46250715Steady-state analysis of enzymes with non-Michaelis-Menten kinetics. The transport mechanism of Na+/K+-ATPase
Q68259654The calmodulin-binding domain as an endogenous inhibitor of the p-nitrophenylphosphatase activity of the Ca2+ pump from human red cells

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