scholarly journals Isolation and partial characterization of a bile canalicular plasma membrane fraction from normal and regenerating rat liver

1975 ◽  
Vol 250 (16) ◽  
pp. 6464-6468
Author(s):  
AE Sirica ◽  
PJ Goldblatt ◽  
JF McKelvy
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Membrane Fraction ◽  
Partial Characterization ◽  
Plasma Membrane Fraction ◽  
Regenerating Rat Liver

scholarly journals CHARACTERIZATION OF RAT LIVER SUBCELLULAR MEMBRANES

1974 ◽  
Vol 60 (2) ◽  
pp. 460-472 ◽  
Author(s):  
David H. DeHeer ◽  
Merle S. Olson ◽  
R. Neal Pinckard
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Nuclear Membrane ◽  
Membrane Fraction ◽  
Cross Reactivity ◽  
Selective Absorption ◽  
Mitochondrial Membranes ◽  
Subcellular Membrane ◽  
Hepatocellular Necrosis

The induction of acute hepatocellular necrosis in rats resulted in the production of complement fixing, IgM autoantibodies directed toward inner and outer mitochondrial membranes, microsomal membrane, lysosomal membrane, nuclear membrane, cytosol, but not to plasma membrane. Utilizing selective absorption procedures it was demonstrated that each subcellular membrane fraction possessed unique autoantigenic activity with little or no cross-reactivity between the various membrane fractions. It is proposed that the development of membrane-specific autoantibodies may provide an immunological marker useful in the differential characterization of various subcellular membranes.

scholarly journals Activation of rat liver plasma-membrane diacylglycerol kinase by vasopressin and phenylephrine

1988 ◽  
Vol 255 (3) ◽  
pp. 923-928 ◽  
Author(s):  
M H Rider ◽  
A Baquet
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Membrane Fraction ◽  
Kinase Activity ◽  
Diacylglycerol Kinase ◽  
Liver Plasma Membrane ◽  
Plasma Membrane Fraction ◽  
In Cells

Plasma-membrane fractions were prepared from the livers of rats injected with 0.15 M-NaCl (controls) or vasopressin (1 nmol/kg body wt.). When assayed in the presence of deoxycholate, vasopressin increased the Vmax. of plasma-membrane diacylglycerol kinase 2-4-fold, and the apparent Km of the enzyme for 1,2-dioleoyl-sn-glycerol was doubled. The effect of vasopressin on the Vmax. of plasma-membrane diacylglycerol kinase was twice as great between pH 7 and 8.5 than at pH 6 or 6.5. Vasopressin doubled the activity of diacylglycerol kinase in the plasma-membrane fraction when the enzyme was assayed with phosphatidylserine rather than deoxycholate as stimulator, and when either 1-stearoyl-2-arachidonoyl-sn-glycerol or 1,2-dioleoyl-sn-glycerol was the substrate. In perfused livers vasopressin (10 nM) increased the Vmax. of plasma-membrane diacylglycerol kinase 2-fold, and phenylephrine (3 microM) gave a similar effect. Vasopressin doubled diacylglycerol kinase activity in hepatocytes that had been preincubated for 55 min, but not in cells that had only been preincubated for 15 min.

Characterization of plasma membrane fraction from filamentous fungus Rhizopus nigricans

2000 ◽  
Vol 439 (7) ◽  
pp. R137-R138
Author(s):  
Helena Lenasi ◽  
Maja Šlajpah ◽  
Maksimiljan Sterle ◽  
Tamara Hudnik-Plevnik ◽  
Katja Breskvar
Keyword(s):  
Plasma Membrane ◽  
Filamentous Fungus ◽  
Membrane Fraction ◽  
Rhizopus Nigricans ◽  
Plasma Membrane Fraction

Isolation and characterization of plasma membranes from bovine carotid arteries

1986 ◽  
Vol 250 (1) ◽  
pp. C65-C75 ◽  
Author(s):  
R. V. Sharma ◽  
R. C. Bhalla
Keyword(s):  
Plasma Membrane ◽  
Cytochrome C ◽  
Membrane Fraction ◽  
Plasma Membranes ◽  
Carotid Arteries ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Cytochrome C Reductase ◽  
Plasma Membrane Fraction

A plasma membrane fraction from bovine carotid arteries has been isolated by extraction of a crude microsomal fraction with a low-ionic-strength buffer containing ATP and Ca2+. This step was followed by sucrose-density-gradient centrifugation in the presence of 0.6 M KCl. The plasma membrane vesicles were enriched 60- to 80-fold in Na+-K+-adenosinetriphosphatase, 5'-nucleotidase, and phosphodiesterase I activities. The final yields of these marker enzymes were 12-18% of the total activities in the postnuclear supernatant, and the protein yield was 100-120 micrograms/g wet wt of carotid arteries. Contamination of the plasma membrane fraction by mitochondria and sarcoplasmic reticulum was low as judged by low activities of succinate--cytochrome-c reductase and NADPH--cytochrome-c reductase, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with smooth muscle-specific actin antibodies showed that the plasma membrane fraction was substantially free from myosin and actin contamination. The plasma membrane vesicles accumulated Ca2+ in the presence of ATP, and the accumulation was increased by calmodulin. Ca2+ accumulated in the presence or absence of calmodulin could be released almost completely from the vesicles by the addition of the Ca2+ ionophore A23187 but not by ethyleneglycol-bis(beta-aminoethylether)-N,N'-tetraacetic acid, indicating that Ca2+ uptake in the presence of ATP is intravesicular. The effects of phosphate and oxalate on Ca2+ uptake in the plasma membranes were different from one another. Phosphate increased Ca2+ uptake in a concentration- and time-dependent manner, and the increase in Ca2+ uptake could be observed as early as 1 min. On the other hand, oxalate at concentrations up to 5 mM did not increase Ca2+ uptake significantly during the 30-min incubation. These plasma membranes can prove useful for the study of ion transport across plasma membranes, hormone binding, characterization of calcium channels, and preparation of antibodies against plasma membrane proteins.

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