Localization of phospholipase Cβ1 on the detergent-resistant membrane microdomain prepared from the synaptic plasma membrane fraction of rat brain

2007 ◽  
Vol 85 (6) ◽  
pp. 1364-1371 ◽  
Author(s):  
Katsutoshi Taguchi ◽  
Haruko Kumanogoh ◽  
Shun Nakamura ◽  
Shohei Maekawa
Keyword(s):  
Plasma Membrane ◽  
Rat Brain ◽  
Membrane Fraction ◽  
Synaptic Plasma Membrane ◽  
Plasma Membrane Fraction ◽  
Membrane Microdomain ◽  
Detergent Resistant Membrane

scholarly journals Purification of the Ca2+-and Mg2+-requiring ATPase from rat brain synaptic plasma membrane

1982 ◽  
Vol 207 (2) ◽  
pp. 225-231 ◽  
Author(s):  
G Hakim ◽  
T Itano ◽  
A K Verma ◽  
J T Penniston
Keyword(s):  
Plasma Membrane ◽  
Rat Brain ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Membrane Fraction ◽  
Synaptic Plasma Membrane ◽  
Human Erythrocyte Membrane ◽  
Specific Antibodies ◽  
Heart Sarcolemma ◽  
Membrane Atpases

A Ca2+-ATPase (Ca2+- and Mg2+-requiring ATPase) was purified from a synaptic plasma-membrane fraction of rat brain. This enzyme had properties similar to those of plasma-membrane Ca2+-ATPases from other organs: its splitting of ATP was dependent on both Ca2+ and Mg2+, it bound in a Ca2+-dependent fashion to calmodulin-Sepharose and it cross-reacted with specific antibodies raised against human erythrocyte-membrane Ca2+-ATPase. It had an apparent Mr of 138 000, similar to those of plasma-membrane ATPases from human erythrocyte and from dog heart sarcolemma. Previous high-Ca2+-affinity ATPases observed in brain had Mr 100 000; in at least one case, such an ATPase probably represented a different type of enzyme, derived from coated vesicles.

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