The ultrastructural localization of transport ATPase in the rat liver at non-bile canalicular plasma membranes

Na,K-ATPase in rat livers was localized cytochemically at the ultrastructural level. The Ernst technique, a method using p-nitrophenylphosphate (pNPP) substrate, was used to demonstrate ouabain-sensitive, K-dependent phosphatase, an enzyme of the Na,K-ATPase reaction sequence. Reaction product was l...

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Bibliographic Details
Published inGastroenterology (New York, N.Y. 1943) Vol. 76; no. 5 Pt 1; p. 988
Main Authors Latham, P S, Kashgarian, M
Format Journal Article
LanguageEnglish
Published United States 01.05.1979
Subjects
Adenosine Triphosphatases - metabolism
Animals
Cell Membrane - enzymology
Histocytochemistry
Liver - enzymology
Liver - ultrastructure
Magnesium
Male
Rats
Sodium-Potassium-Exchanging ATPase - metabolism
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Summary:Na,K-ATPase in rat livers was localized cytochemically at the ultrastructural level. The Ernst technique, a method using p-nitrophenylphosphate (pNPP) substrate, was used to demonstrate ouabain-sensitive, K-dependent phosphatase, an enzyme of the Na,K-ATPase reaction sequence. Reaction product was localized predominantly on the sinusoidal and non-bile canalicular (intercellular) surfaces. This localization contrasts with previous histo-chemical studies using ATP substrate and with models that have considered the transport enzyme to be localized at the canalicular surface. If Na,K-ATPase is of importance in bile salt independent flow, a significant presence of the enzyme at sites other than the canalicular membrane suggests that a paracellular movement of sodium and water into the canaliculus must be considered.
ISSN:0016-5085