The Denaturation of Proteins by Synthetic Detergents and Bile Salts

All the synthetic detergents and bile salts I have tried denature proteins such as hemoglobin and egg albumin at the isoelectric point 1 and keep the denatured isoelectric protein in solution. Some detergents in sufficiently high concentration can prevent the precipitation of denatured protein by trichloracetic acid, tungstic acid, and acid ferric sulfate. In fact, the origin of the present investigation was the observation that a detergent used to clean test tubes containing hemoglobin precipitated by trichloracetic acid dissolved the precipitated hemoglobin. The synthetic detergents and the bile salts all have the same general type of hydrophobic-hydrophilic structure. Each consists of a large hydrophobic part with a small hydrophilic part attached to it. The detergents are extremely surface active and their hydrophobic groups can combine with hydrophobic particles to give these particles a coating of hydrophilic groups. Since the synthetic detergents and bile salts differ widely in their specific chemical structures, the denaturation of proteins and the solution of denatured protein by synthetic detergents and bile salts must be attributed to the one property these compounds have in common, their type of hydrophobic-hydrophilic structure. There is a great variety of synthetic detergents available commercially partly because each type of detergent is patented and partly because by variation in the specific structures of the detergents, detergents have been developed which are particularly suited for specific industrial uses. Although the synthetic detergents were originally introduced as soap substitutes their industrial uses are now very varied. As soap substitutes and