The phospholipid molecular species of canine myocardial sarcoplasmic reticulum were identified by fast atom bombardment mass spectrometry, reverse-phase high-performance liquid chromatography, and other conventional techniques. Cardiac sarcoplasmic reticulum contains 1.4 μmol of lipid Pi/mg of protein which is comprised of 53% plasmalogen. Cardiac sarcoplasmic reticulum ethanolamine glycero-phospholipid contains 73% plasmalogen that is predominantly comprised of moieties with 18-carbon vinyl ethers at the sn-1 position and arachidonic acid at the sn-2 position. In contrast, canine skeletal muscle sarcoplasmic reticulum contains only 19% plasmalogen that is predominantly comprised of ethanolamine plasmalogen (78% of skeletal muscle sarcoplasmic reticulum ethanolamine glycerophospholipid) with arachidonic and docosatetraenoic acids at the sn-2 position. The possibility that tetraenoic ethanolamine plasmalogens in both cardiac and skeletal muscle sarcoplasmic reticulum facilitate calcium translocation by their propensity for adopting a hexagonal II conformation at physiologic temperatures is discussed.

Original languageEnglish
Pages (from-to)1662-1668
Number of pages7
Issue number7
StatePublished - Mar 1 1985


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