AI Article Synopsis
- The study investigates how the non-ionic detergent Triton X-100 affects the membrane structures of three different biological systems: rabbit sarcoplasmic reticulum, Halobacterium purple membrane, and gramicidin A-phosphatidylcholine liposomes.
- It measures changes in turbidity and analyzes chemical compositions to assess the solubilization effects on proteins and lipids, comparing these findings with earlier research on other membranes.
- The research proposes a three-stage model to explain the interaction between membranes and Triton X-100, detailing the incorporation of surfactant, disruption of the bilayer, and the separation of lipid from protein.
Article Abstract
The solubilizing effects of the non-ionic detergent Triton X-100 have been examined on three membranous systems, namely rabbit sarcoplasmic reticulum, Halobacterium purple membrane and gramicidin A-phosphatidylcholine liposomes. The loss of membrane structure has been assessed through changes in suspension turbidity, while chemical analysis has revealed the differential solubilization of proteins and lipids. Solubilization data obtained on the above three systems are compared with previously published values concerning other membrane preparations. Also, solubilization of sarcoplasmic reticulum by Triton X-100 is monitored by Fourier-transform infrared spectroscopy and, similarly, purple membrane-surfactant interaction is studied using visible spectroscopy. The biochemical and spectroscopic data may be rationalized assuming a three-stage model of membrane-detergent interaction, incorporation of surfactant monomers into the membrane; disruption of the bilayer into mixed micelles, and separation of lipid and protein.
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