The effect of phospholipase D on the function of fragmented sarcoplasmic reticulum.
Incubations of fresh preparations of fragmented sarcoplasmic reticulum (FSR) were carried out at pH 5.7. This pH was necessary for hydrolysis of phospholipids by phospholipase D. The pH did not influence calcium uptake or the activity of calcium-stimulated ATPase of FSR. Treatment of FSR with phospholipase D caused hydrolysis of the membrane phospholipids. The phosphatidic acid produced remained bound to the membrane. Increasing phospholipid cleavage was paralleled by loss of calcium uptake, which was complete when about two-thirds of the membrane phospholipids were hydrolyzed.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D002474:Cell-Free System; D006863:Hydrogen-Ion Concentration; D008563:Membrane Lipids / Q000378:metabolism; D010740:Phospholipases / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D008563:Membrane Lipids; D010743:Phospholipids; D010740:Phospholipases; D000251:Adenosine Triphosphatases; D002118:Calcium