The Ultrastructural Localization of Transport ATPase in the Rat Liver at Nonbile 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 ouabainsensitive, 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 histochemical studies using ATP substrate and with models that have considered the transport enzyme to be localized at the canalicular surface. I f 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 conaliculus must be considered. © 1979, American Gastroenterological Association. All rights reserved.
Latham, P., & Kashgarian, M. (1979). The Ultrastructural Localization of Transport ATPase in the Rat Liver at Nonbile Canalicular Plasma Membranes. Gastroenterology, 76 (5). http://dx.doi.org/10.1016/S0016-5085(79)91330-1