The kinetics of protein salting-out: precipitation of yeast enzymes by ammonium sulfate.
Protein solubility can be adequately represented by the classical Cohn equation for the salting-out of alcohol dehydrogenase and fumarase from clarified yeast homogenate with ammonium sulfate. However, the constant beta in this equation is a function of the contacting procedure employed. The kinetics of continuous salting-out were similar for alcohol dehydrogenase and fumarase. The overall rate equation for precipitation had a variable order which was high initially, up to 3.1, but approached unity on completion of precipitation. This was followed by a partial resolution stage which was first order with respect to the concentration driving force. Precipitate particle size was estimated as 0.5 to 5 mum with continuous flow precipitation producing the largest particles.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D005649:Fumarate Hydratase / Q000302:isolation & purification*; D006836:Hydro-Lyases / Q000302:isolation & purification*; D007700:Kinetics; D010316:Particle Size; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012995:Solubility
D000429:Alcohol Oxidoreductases; D006836:Hydro-Lyases; D005649:Fumarate Hydratase; D000645:Ammonium Sulfate