WATER-SOLUBLE PROTEINS DO NOT BIND OCTYL GLUCOSIDE AS JUDGED BY MOLECULAR-SIEVE CHROMATOGRAPHIC TECHNIQUES

It is well known that the non-ionic detergent octyl glucoside (1-O-n-octyl-β-d-glucopyranoside) solubilizes biological membrane components. It forms complexes with membrane-spanning proteins by hydrophobic interactions and it forms mixed micelles with membrane lipids. In contrast, non-ionic detergents usually do not bing to water-soluble proteins. According to a recent report, substantial and cooperative binding of octyl glucoside to several water-soluble proteins does occur near the critical micelle concentration. However, data have been obtained that contradict this report. No decrease was found in the elution volumes of five water-soluble proteins on molecular sieve chromatography on two Superose columns in tandem when 35 mM octyl glucoside was included in the eluent. No binding of the detergent to these proteins was observed at 20 or 22.5 mM octyl glucoside on molecular sieve chromatography on a TSK SW guard column as determined by differential refractometry and UV spectrophotometry of the proteins in the absence or presence of octyl glucoside. The experiments were done with the same buffer system and with six of the proteins used in the reported study. It is concluded that, as expected, there is no binding of octyl glucoside to water-soluble proteins above the detection limit (0.1 g detergent/g protein) of the refractometric method. The binding of, on average, 1.3 ± 0.2 g of detergent per gram of was observed at 20 mM octyl glucoside in the reported study is not consistent with the present results. © 1990.