Evidence for membrane microheterogeneity in the sarcoplasmic reticulum of fast twitch skeletal muscle.

Sarcoplasmic reticulum (SR) from rabbit back muscles can be readily subfractionated into two morphologically and compositionally different vesicular populations, SRH (heavy) and SRL (light) derived from terminal cisternae and longitudinal SR, respectively. Polyacrylamide gels indicate that SRH contains most of the calsequestrin. Quantitation of freeze-fractured isolated preparations reveals that, while differences in vesicular dimensions are seen in SRH and SRL, the intramembrane particle (Ca2+ ATPase) density is identical. Phospholipid headgroup composition is the same in SRH and SRL, but fatty acyl moieties show significant differences in the ratio of saturated to unsaturated phospholipids in the two fractions. The vesicular dimensions of the purified Ca2+-ATPases, SRHP and SRLP, from the two fractions are identical, but the freeze-fracture particle density is higher in the SRLP fraction. The phospholipid composition remains similar after purification, but the differences in phospholipid fatty acyl composition of the preparations are maintained. SRH and SRHP contain almost twice as much of the unsaturated species as compared to SRL and SRLP. Differences in intramembrane particle density in purified fractions, thermotropic segregation of particles in freeze-fractured purified fractions, as well as differences in turnover of the acyl phosphate, appear to reflect the differences in fatty acyl chain composition of the two SR fractions and provide evidence of microheterogeneity in lipid-protein environment of the SR.