Naunyn-Schmiedeberg's Archives of Pharmacology

, Volume 282, Issue 3, pp 279–293 | Cite as

Effects of lipid-modification on the isolated membrane of catecholamine storage vesicles

  • G. Taugner
  • A. Wähler


The ATPase activity of isolated membranes of catecholamine storage vesicles from adrenal medulla remains unimpaired on hydrolysis of phospholipids by phospholipase A as long as the products of lipolysis—fatty acids and lysophosphatidyl derivatives—remain in contact with the protein.

Washing the phospholipase A-digested preparation with bovine serum albumin preferentially removes the fatty acids, inhibits the specific activity of the ATPase by 10% and reduces the rate of the net uptake of catecholamine.

After treatment with phospholipase A about 50% of the sedimentable membrane protein is lost. The supernatant does not display any ATPase activity indicating that dissolution of the membrane structure by lipid deprivation causes the function to cease.

Oleic acid slightly increases the ATPase activity of native isolated membranes and more markedly that of membranes previously partially deprived of phospholipids by treatment with phospholipase A and subsequent washing with serum albumin. The net uptake of catecholamine is inhibited completely by oleic acid. Lysolecithin leaves the ATPase activity of isolated membranes unimpaired, but it antagonizes the stimulant effect of oleic acid on the ATPase activity of the membrane preparation partially deprived of phospholipids.

Key words

ATPase Activity Transportmechanism Phospholipase A Lysolecithin Oleic Acid 


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Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • G. Taugner
    • 1
  • A. Wähler
    • 1
  1. 1.Abteilung PhysiologieMax-Planck-Institut für Medizinische ForschungHeidelbergGermany

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