n-Octyl-b-D-Glucoside (Molecular Biology)

This detergent has a high critical micelle concentration (cmc) of 23 nM and has been used to solubilize and reconstitute many integral membrane proteins efficiently. The special advantage in using this detergent is in the efficient postsolubilization removal of the detergent by dialysis. It is only mildly denaturing, which makes it highly efficient in solubilizing integral membrane proteins, such as the nicotinic acetylcholine receptor and those for opioids, GABAa (1-3), and the photoreceptor guanylate cyclase (4). However, the relative inefficiency of this detergent in solubilizing plasma membrane lipids (as compared to CHAPS and dodecylmaltoside, see Detergents), makes it inappropriate for solubilizing and reconstituting the heavily lipid-dependent serotonin 1A receptor (5, 6). Nevertheless, because of its weakly denaturing property, this detergent has been efficiently used to obtain active preparations of other solubilized membrane proteins, such as the mitochondrial membrane protein carnitine palmitoyltransferase I (7) or the GPI-anchored proteins (8). It is also a popular detergent in X-ray crystallography, where it is used to crystallize solubilized membrane proteins. Typical examples of such studies include the solubilization of the bifunctional enzyme fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase (9), and prostaglandin H synthase-1 (10).

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