Modulation of the Ca2+/Mg2+-ATPase Activity of Synaptosomal Plasma Membrane Vesicles by the Hypothalamic Hypophysary Na+/K+-ATPase Inhibitory Factor (HHIF)

1994 ◽  
pp. 783-786 ◽  
Author(s):  
M. Ricote ◽  
E. Garcia ◽  
C. Gutierrez ◽  
J. Sancho
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Membrane Vesicles ◽  
Inhibitory Factor ◽  
Plasma Membrane Vesicles ◽  
Synaptosomal Plasma Membrane

Effect of detergents on the H+-ATPase activity of inside-out and right-side-out plant plasma membrane vesicles

1990 ◽  
Vol 1021 (2) ◽  
pp. 133-140 ◽  
Author(s):  
Michael Gjedde Palmgren ◽  
Marianne Sommarin ◽  
Peter Ulvskov ◽  
Christer Larsson
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Inside Out ◽  
Plant Plasma Membrane

Effect of antimicrobial peptides on ATPase activity and proton pumping in plasma membrane vesicles obtained from mycobacteria

Peptides ◽  
2012 ◽  
Vol 36 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Paola Santos ◽  
Aldemar Gordillo ◽  
Luis Osses ◽  
Luz-Mary Salazar ◽  
Carlos-Yesid Soto
Keyword(s):  
Plasma Membrane ◽  
Antimicrobial Peptides ◽  
Atpase Activity ◽  
Membrane Vesicles ◽  
Proton Pumping ◽  
Plasma Membrane Vesicles

scholarly journals Characteristics of the Ca2+ pump and Ca2+-ATPase in the plasma membrane of rat myometrium

1988 ◽  
Vol 252 (1) ◽  
pp. 215-220 ◽  
Author(s):  
A Enyedi ◽  
J Minami ◽  
A J Caride ◽  
J T Penniston
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Calcium Uptake ◽  
Limited Proteolysis ◽  
Membrane Vesicles ◽  
Calcium Pump ◽  
Ionophore A23187 ◽  
Plasma Membrane Vesicles ◽  
Active Calcium ◽  
Stimulation Of

A plasma membrane-enriched fraction from rat myometrium shows ATP-Mg2+-dependent active calcium uptake which is independent of the presence of oxalate and is abolished by the Ca2+ ionophore A23187. Ca2+ loaded into vesicles via the ATP-dependent Ca2+ uptake was released by extravesicular Na+. This showed that the Na+/Ca2+ exchange and the Ca2+ uptake were both occurring in plasma membrane vesicles. In a medium containing KCl, vanadate readily inhibited the Ca2+ uptake (K1/2 5 microM); when sucrose replaced KCl, 400 microM-vanadate was required for half inhibition. Only a slight stimulation of the calcium pump by calmodulin was observed in untreated membrane vesicles. Extraction of endogenous calmodulin from the membranes by EGTA decreased the activity and Ca2+ affinity of the calcium pump; both activity and affinity were fully restored by adding back calmodulin or by limited proteolysis. A monoclonal antibody (JA3) directed against the human erythrocyte Ca2+ pump reacted with the 140 kDa Ca2+-pump protein of the myometrial plasma membrane. The Ca2+-ATPase activity of these membranes is not specific for ATP, and is not inhibited by mercurial agents, whereas Ca2+ uptake has the opposite properties. Ca2+-ATPase activity is also over 100 times that of calcium transport; it appears that the ATPase responsible for transport is largely masked by the presence of another Ca2+-ATPase of unknown function. Measurements of total Ca2+-ATPase activity are, therefore, probably not directly relevant to the question of intracellular Ca2+ control.

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