The effect of phospholipids on the thermostability of the ATPase from locust and crayfish sarcoplasmic reticulum.
The temperature dependence of delipidated and phospholipid-replaced ATPase from crayfish and locust sarcoplasmic reticulum (SR) was studied. Removal of approx. 85% of the phospholipids present in locust SR considerably decreased the temperature optimum of the ATPase, indicating that the thermostability of the ATPase is dependent on the phospholipids surrounding the enzyme. Addition of distearoylphosphatidylcholine to the delipidated ATPase from locust and crayfish SR increased the thermostability, whereas a decrease could be observed upon addition of dilinoleoyl- and dimyristoylphosphatidylcholine. These results suggest that the thermostability of the ATPase might be affected by the conformation of the fatty acyl chains in the microenvironment of the enzyme.
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D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D003400:Astacoidea / Q000201:enzymology*; D004355:Drug Stability; D006110:Grasshoppers / Q000201:enzymology*; D006358:Hot Temperature; D007700:Kinetics; D008563:Membrane Lipids / Q000032:analysis; D009132:Muscles / Q000201:enzymology; D010743:Phospholipids / Q000494:pharmacology*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013045:Species Specificity
D008563:Membrane Lipids; D010743:Phospholipids; D000251:Adenosine Triphosphatases