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dc.contributor.authorSachs, Georgeen
dc.date.accessioned2019-02-15T14:19:47Z
dc.date.available2019-02-15T14:19:47Z
dc.date.issued1981
dc.identifier.urihttp://hdl.handle.net/1842/33803
dc.description.abstracten
dc.description.abstractThe microsomal fraction of both dog and hog gastric mucosa contains a K⁺ activated ATPase. ATP phosphorylates a peptide of c̅ 100,000 Mᵣ in both species, and dephosphorylation is stimulated by K⁺. By a combination of differential and zonal density gradient centrifugation a membrane fraction is produced containing almost exclusively this peptide region. These vesicles, upon the addition of ATP, take up H⁺ and extrude K⁺. The action of ionophores such as nigericin or valinomycin and the uptake of lipid permeable anions such as thiocyanate or anilino-naphthosulfonic acid indicate the lack of a potential difference during transport. Reconstitution of this material into a planar bilayer indicates that ATP activates a K⁺ conductance and hence, in the presence of K⁺ also a low potential difference is observed. These data suggest that this H⁺ pump is non-electrogenic as prepared in the vesicular form. Using an antibody obtained from rabbits immunized with the highly purified membrane fractions, it was demonstrated that this membrane was derived uniquely from gastric parietal cells. Hence, based on the ability of this ATPase to actively transport H⁺, its cellular origin and on the well known K⁺ requirement for acid secretion in amphibia and mammals, it is concluded that this ATPase is a component of the HCl secretory mechanism of gastric mucosa.en
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dc.publisherThe University of Edinburghen
dc.relation.ispartofAnnexe Thesis Digitisation Project 2019 Block 22en
dc.relation.isreferencedbyen
dc.titleCharacterization of gastric ATPase vesicle transporten
dc.typeThesis or Dissertationen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnameDSc Doctor of Scienceen


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