AbstractImmunological homology was investigated between Heterosigma akashiwo (a marine alga) Na+-activated ATPase and animal Na+,K+-ATPase. The former polypeptide [(1989) Plant Cell Physiol. 30, 923-928] reacted with anti-serum raised against the amino-terminal half of the pig kidney Na+,K+-ATPase α subunit. It is suggested that the Na+,K+-ATPase epitope within the amino-terminal region is conserved in the plant Na+-activated ATPase, and the region containing the epitope may be important for Na ion transport
AbstractcDNAs complementary to pig kidney mRNAs coding for α- and β-subunits of Na+,K+-ATPase were c...
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. To obtai...
AbstractPrimary Na+ transport has been essentially attributed to Na+/K+ pump. However, there are fun...
AbstractImmunological homology was investigated between Heterosigma akashiwo (a marine alga) Na+-act...
AbstractA polyclonal antibody against the Na+,K+-ATPase holoenzyme was prepared. This antibody recog...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
AbstractWe cloned novel Na+-ATPase (HANA) cDNA from marine alga Heterosigma akashiwo. The full-lengt...
AbstractTo study the topology of Na+,K+-ATPase monoclonal antibodies (MAbs) specific for membrane-bo...
AbstractProton transport by the vanadate-sensitive ATPase in plasma membrane (PM) vesicles from the ...
AbstractThe ATP-supported 22NA+ uptake by plasma membrane vesicles from the marine microalga, Platym...
AbstractUsing four oligopeptide-specific polyclonal antibodies, we mapped the α subunit ofNa,K-ATPas...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
AbstractMembrane-bound (Na,K)-ATPases were exposed to limited papain digestion. We could not find th...
AbstractThe sodium pump or Na,K-ATPase, maintains the Na+ and K+ gradients across eukaryotic cell me...
Highly purified plasma membranes were isolated from Heterosigma akashiwo cells, a marine raphidophyc...
AbstractcDNAs complementary to pig kidney mRNAs coding for α- and β-subunits of Na+,K+-ATPase were c...
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. To obtai...
AbstractPrimary Na+ transport has been essentially attributed to Na+/K+ pump. However, there are fun...
AbstractImmunological homology was investigated between Heterosigma akashiwo (a marine alga) Na+-act...
AbstractA polyclonal antibody against the Na+,K+-ATPase holoenzyme was prepared. This antibody recog...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
AbstractWe cloned novel Na+-ATPase (HANA) cDNA from marine alga Heterosigma akashiwo. The full-lengt...
AbstractTo study the topology of Na+,K+-ATPase monoclonal antibodies (MAbs) specific for membrane-bo...
AbstractProton transport by the vanadate-sensitive ATPase in plasma membrane (PM) vesicles from the ...
AbstractThe ATP-supported 22NA+ uptake by plasma membrane vesicles from the marine microalga, Platym...
AbstractUsing four oligopeptide-specific polyclonal antibodies, we mapped the α subunit ofNa,K-ATPas...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
AbstractMembrane-bound (Na,K)-ATPases were exposed to limited papain digestion. We could not find th...
AbstractThe sodium pump or Na,K-ATPase, maintains the Na+ and K+ gradients across eukaryotic cell me...
Highly purified plasma membranes were isolated from Heterosigma akashiwo cells, a marine raphidophyc...
AbstractcDNAs complementary to pig kidney mRNAs coding for α- and β-subunits of Na+,K+-ATPase were c...
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. To obtai...
AbstractPrimary Na+ transport has been essentially attributed to Na+/K+ pump. However, there are fun...