Rabbit distal colon epithelium: I. Isolation and characterization of basolateral plasma membrane vesicles from surface and crypt cells

1989 ◽  
Vol 110 (2) ◽  
pp. 147-162 ◽  
Author(s):  
Hubert Wiener ◽  
Klaus Turnheim ◽  
Carel H. van Os
Keyword(s):  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Distal Colon ◽  
Plasma Membrane Vesicles ◽  
Isolation And Characterization ◽  
Basolateral Plasma Membrane ◽  
Distal Colon Epithelium ◽  
Crypt Cells

scholarly journals Isolation and characterization of luminal and basolateral plasma membrane vesicles from the medullary thick ascending loop of Henle

1996 ◽  
Vol 50 (3) ◽  
pp. 1051-1057 ◽  
Author(s):  
Amel Attmane-Elakeb ◽  
Régine Chambrey ◽  
Michel Tsimaratos ◽  
Françoise Leviel ◽  
Anne Blanchard ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Loop Of Henle ◽  
Plasma Membrane Vesicles ◽  
Isolation And Characterization ◽  
Basolateral Plasma Membrane

The isolation and characterization of right-side-out plasma membrane vesicles from barley aleurone cells

Lipids ◽  
1999 ◽  
Vol 34 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Kim M. Robbins ◽  
Narasimhan Bhuvarahamurthy ◽  
Gay Pliska-Matyshak ◽  
Pushpalatha P. N. Murthy
Keyword(s):  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Aleurone Cells ◽  
Isolation And Characterization ◽  
Barley Aleurone

Characterization of a glutamine/proton cotransporter from Ricinus communis roots using isolated plasma membrane vesicles

1994 ◽  
Vol 91 (4) ◽  
pp. 623-630
Author(s):  
Kim Weston ◽  
J. L. Hall ◽  
Lorraine E. Williams
Keyword(s):  
Plasma Membrane ◽  
Ricinus Communis ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles

scholarly journals Albumin binding of unconjugated [3H]bilirubin and its uptake by rat liver basolateral plasma membrane vesicles

1996 ◽  
Vol 316 (3) ◽  
pp. 999-1004 ◽  
Author(s):  
Lorella PASCOLO ◽  
Savino DEL VECCHIO ◽  
Ronald K. KOEHLER ◽  
J. Enrique BAYON ◽  
Cecile C. WEBSTER ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Basolateral Membrane ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Experimental Conditions ◽  
Saturation Kinetics ◽  
Basolateral Plasma Membrane ◽  
Component C ◽  
Uptake Studies

Using highly purified unconjugated [3H]bilirubin (UCB), we measured UCB binding to delipidated human serum albumin (HSA) and its uptake by basolateral rat liver plasma membrane vesicles, in both the absence and presence of an inside-positive membrane potential. Free UCB concentrations ([Bf]) were calculated from UCB–HSA affinity constants (K´f), determined by five cycles of ultrafiltration through a Centricon-10 device (Amicon) of the same solutions used in the uptake studies. At HSA concentrations from 12 to 380 μM, K´f (litre/mol) was inversely related to [HSA], irrespective of the [Bt]/[HSA] ratio. K´f was 2.066×106+(3.258×108/[HSA]). When 50 mM KCl was iso-osmotically substituted for sucrose, the K´f value was significantly lower {2.077×106+(1.099×108/[HSA])}. The transport occurred into an osmotic-sensitive space. Below saturation ([Bf] ⩽ 65 nM), both electroneutral and electrogenic components followed saturation kinetics with respect to [Bf], with Km values of 28±7 and 57±8 nM respectively (mean±S.D., n = 3, P < 0.001). The Vmax was greater for the electrogenic than for the electroneutral component (112±12 versus 45±4 pmol of UCB·mg-1 of protein·15 s-1, P < 0.001). Sulphobromophthalein trans-stimulated both electrogenic (61%) and electroneutral (72%) UCB uptake. These data indicate that: (a) as [HSA] increases, K´f decreases, thus increasing the concentration of free UCB. This may account for much of the enhanced hepatocytic uptake of organic anions observed with increasing [HSA]. (b) UCB is taken up at the basolateral membrane of the hepatocyte by two systems with Km values within the range of physiological free UCB levels in plasma. The electrogenic component shows a lower affinity and a higher capacity than the electroneutral component. (c) It is important to calculate the actual [Bf] using a K´f value determined under the same experimental conditions (medium and [HSA]) used for the uptake studies.

Taurocholate transport by basolateral plasma membrane vesicles isolated from human liver

Hepatology ◽  
1989 ◽  
Vol 10 (4) ◽  
pp. 447-453 ◽  
Author(s):  
Donald A. Novak ◽  
Frederick C. Ryckman ◽  
Frederick J. Suchy
Keyword(s):  
Plasma Membrane ◽  
Human Liver ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Basolateral Plasma Membrane ◽  
Taurocholate Transport

scholarly journals Characterization of the plasma-membrane calcium pump from Trypanosoma cruzi

1995 ◽  
Vol 306 (1) ◽  
pp. 299-303 ◽  
Author(s):  
G Benaim ◽  
S N J Moreno ◽  
G Hutchinson ◽  
V Cervino ◽  
T Hermoso ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Mammalian Cells ◽  
Membrane Vesicles ◽  
High Sensitivity ◽  
Bovine Brain ◽  
Calcium Pump ◽  
Plasma Membrane Vesicles ◽  
P Type

Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh, Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca(2+)-ATPases of different trypanosomatids differ from the Ca2+ pumps present in mammalian cells, Trypanosoma cruzi plasma-membrane Ca(2+)-ATPase shares several characteristics with the Ca2+ pumps present in other systems. This enzyme could be partially purified from epimastigote plasma-membrane vesicles using calmodulin-agarose affinity chromatography. The activity of the partially purified enzyme was stimulated by T. cruzi or bovine brain calmodulin. In addition, the enzyme cross-reacted with antiserum and monoclonal antibody 5F10 raised against human red-blood-cell Ca(2+)-ATPase, has a molecular mass of 140 kDa and forms Ca(2+)-dependent hydroxylamine-sensitive phosphorylated intermediates. These results, together with its high sensitivity to vanadate, indicate that this enzyme belongs to the P-type class of ionic pumps.

Sign in / Sign up

Export Citation Format

Share Document