PERSPECTIVES AND OVERVIEW For the better part of the century, a common practice among biologists and biochemists, when they isolate a biologically active entity (e.g. an enzyme activity) or dissect an organelle out of a cell, has been to add a high concentration of sucrose ( ï¿½ 1 M) or glycerol ( ï¿½ 10%) to the medium 67 1056-8700/93/0610-0067$02.00 TIMASHEFF in order to keep the activity stabilized or the organelle functional. For just as long, when isolating enzymes and other proteins, biochemists have used high concentrations (1-4 M) of salts, most commonly ammonium sulfate, to precipitate the proteins. This process has been called salting-out (32). Similarly, investigators have known that addition of concentrated urea (8 M) or guanidine hydrochloride (GuaHCl) (6 M) leads to the denaturation of proteins (enzymes), i.e. a loss of their biochemical activity, and a drastic alteration in solution properties. Researchers interpreted these obserÂ vations to represent an uncoiling of the native structure of proteins (61). The mechanisms of the salting-out and denaturation processes have been the subject of investigations for well over 50 years, and several excellent reviews explore these areas (14, 40, 64, 65, 89, 91). Precipitation by salts has been analyzed in
Annual Review of Biophysics – Annual Reviews
Published: Jun 1, 1993
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