ATP synthase from rat liver plasma membrane
نویسندگان
چکیده
منابع مشابه
Evidence for Histidine Residues on Plasma Membrane Phosphatidate Phosphohydrolase from Rat Liver
Objective(s) Phosphatidate phosphohydrolase (PAP) catalyzes the dephosphorylation of phosphatidic acid to yield Pi and diacylglycerol. Two different forms of PAP in rat hepatocyte have been reported. PAP1 is located in cytosolic and microsomal fractions and participates in the synthesis of triacylglycerols, phosphatidylcholine, and phosphatidylethanolamine, whereas the other form of phosphati...
متن کاملATP-dependent S-(2,4-dinitrophenyl)glutathione transport in canalicular plasma membrane vesicles from rat liver.
Uptake of the thioether S-(2,4-dinitrophenyl)glutathione (DNPSG) in canalicular plasma membrane vesicles from rat liver is enhanced in the presence of ATP and exhibits an overshoot with a transient 5.5-fold accumulation of DNPSG. Stimulation by ATP is not caused by the generation of a membrane potential, based on responses of the indicator dye oxonol V. ATP-dependent uptake has an apparent Km o...
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The present study identifies and characterizes a novel ATP-dependent bile-salt transport system in isolated canalicular rat liver plasma-membrane (cLPM) vesicles. ATP (1-5 mM) stimulated taurocholate uptake into cLPM vesicles between 6- and 8-fold above equilibrium uptake values (overshoot) and above values for incubations in the absence of ATP. The ATP-dependent portion of taurocholate uptake ...
متن کاملATP-dependent transport of unconjugated bilirubin by rat liver canalicular plasma membrane vesicles.
The transport of highly purified 3H-labelled unconjugated bilirubin (UCB) was investigated in rat liver plasma membrane vesicles enriched in the canalicular domain and found to be stimulated (more than 5-fold) by the addition of ATP. Other nucleotides, such as AMP, ADP, GTP and a non-hydrolysable ATP analogue (adenosine 5'-[alpha, beta-methylene] triphosphate), did not stimulate [3H]UCB transpo...
متن کاملenzymological characteristics of plasma membrane phosphatidate phosphohydrolase (pap2) from rat liver
phosphatidate phosphohydrolase (pap2b, fraction b) was purified from the plasma membrane ofrat liver cells. the km for the surface concentration of phosphatidic acid was 0.43 mol%. the subunit of theenzyme had an m.w. of 33.8 kda using sodium dodecyl sulfate polyacrylamide gel electrophoresis. thenative enzyme shows a molecular weight of 182 kda in a gel filtration column packed with sephacryl ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2012
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2012.06.059