Plasma membranes of the rat liver. Isolation and enzymatic characterization of a fraction rich in bile canaliculi. Academic Article uri icon


MeSH Major

  • Adenosine Triphosphatases
  • Alkaline Phosphatase
  • Cell Membrane
  • Cytochromes
  • Glucose-6-Phosphatase
  • Liver
  • Nucleotidases


  • A method is described for the rapid isolation of a plasma membrane fraction containing a high concentration of intact bile canaliculi from the rat liver. Isolated bile canaliculi retain most of the ultrastructural features exhibited in the intact liver cell. The final fraction contains 5'-nucleotidase activity at approximately the same concentration as that in previous preparations of plasma membranes. In the presence of 0.01 M Mg(++), 5'-nucleotidase exhibits a double pH optimum at pH values of 7.5 and 9.5. The activities of glucose-6-phosphatase and alkaline phosphatase are present in low amounts. Cytochrome P-450 is not detectable. Na(+)-K(+)-activation of ATPase is observed to the extent of 20-36% in about half of the assays. The availability of a method for preparation of intact bile canaliculi should prove useful for studying the biochemical events associated with the transport of bile constituents into canaliculi.

publication date

  • April 1969



  • Academic Article



  • eng

PubMed Central ID

  • PMC2107735

PubMed ID

  • 4304740

Additional Document Info

start page

  • 124

end page

  • 32


  • 41


  • 1