Unknown

Dataset Information

0

Highly purified bile-canalicular vesicles and lateral plasma membranes isolated from rat liver on Nycodenz gradients. Biochemical and immunolocalization studies.


ABSTRACT: 1. A liver canalicular plasma-membrane fraction enriched 115-155-fold in five marker enzymes relative to the tissue homogenate was obtained by sonication of liver plasma membranes followed by fractionation in iso-osmotic Nycodenz gradients. 2. Two lateral-plasma membrane fractions were also collected by this procedure; the lighter-density fraction was still associated with canalicular membranes, as assessed by enzymic and polypeptide analysis. 3. The polypeptide composition of the domain-defined plasma-membrane fractions was evaluated. It was demonstrated by immunoblotting that the 41 kDa alpha-subunit of the inhibitory G-protein, associated in high relative amounts with canalicular plasma-membrane fractions, was partially lost in the last stage of purification; however, this subunit was retained by lateral plasma membranes. 4. Antibodies to the proteins of bile-canalicular vesicles were shown to localize to the hepatocyte surface in thin liver sections examined by immunofluorescent and immuno-gold electron microscopy. Two subsets of antigens were identified, one present on both sinusoidal and canalicular plasma-membrane domains and another, by using antisera pre-absorbed with sinusoidal plasma membranes, that was confined to the bile-canalicular domain.

SUBMITTER: Ali N 

PROVIDER: S-EPMC1149531 | biostudies-other | 1990 Oct

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC5827637 | biostudies-literature
| S-EPMC1132698 | biostudies-other
| S-EPMC1147784 | biostudies-other
| S-EPMC1172759 | biostudies-other
| S-EPMC3807460 | biostudies-literature
| S-EPMC5034288 | biostudies-literature
| S-EPMC5665972 | biostudies-literature
| S-EPMC2947599 | biostudies-literature
| S-EPMC3430690 | biostudies-literature
| S-EPMC1257697 | biostudies-literature