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  • Title: Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids.
    Author: Miljanich GP, Brown MF, Mabrey-Gaud S, Dratz EA, Sturtevant JM.
    Journal: J Membr Biol; 1985; 85(1):79-86. PubMed ID: 4020856.
    Abstract:
    High sensitivity, differential scanning calorimetry studies of bovine retinal rod outer segment (ROS) disk membranes and aqueous dispersions of the extracted ROS phospholipids have been performed. ROS disk membranes were found to exhibit a broad peak of excess heat capacity with a maximum at less than about 3 degrees C, ascribable to a gel-to-liquid crystalline phase transition of a fraction of the phospholipids. A similar thermotropic transition was observed for aqueous dispersions of the total extracted and purified ROS phospholipids. Comparison of the results obtained for the dispersion of total ROS phospholipids to those of the purified head group fractions suggests that the thermotropic behavior reflects a gel-to-liquid crystalline transition, leading to lateral phase separation, involving those phosphatidylcholine (PC) molecules containing saturated fatty acyl chains, possibly together with the highest melting ROS phosphatidylethanolamine (PE) and phosphatidylserine (PS) components. The interpretation of the thermal behavior of the ROS disk membranes depends on whether the transition is assumed to derive from the ROS PC and/or PE/PS fractions, and whether the transbilayer arrangement of the ROS phospholipids is assumed to be symmetric or asymmetric. The calorimetric data can be simply explained in terms of an asymmetric distribution of the major ROS disk membrane phospholipids (G.P. Miljanich et al., J. Membrane Biol. 60:249-255, 1981). In this case, the transition would arise from the PE/PS fractions in the outer ROS disk membrane monolayer, and the anticipated transition from the PC in the inner monolayer would be broadened due to interaction with cholesterol. For the ROS membranes at higher temperatures, two additional, irreversible transitions are observed at 57 and 72 degrees C, corresponding to the thermal denaturation of opsin and rhodopsin, respectively.
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