Elution of exocellular enzymes from Saccharomyces fragilis and Saccharomyces cerevisiae.
Weimberg, Ralph (Northern Regional Research Laboratory, Peoria, Ill.), and William L. Orton. Elution of exocellular enzymes from Saccharomyces fragilis and Saccharomyces cerevisiae. J. Bacteriol. 91:1-13. 1966.-Invertase and acid phosphatase are repressible exocellular enzymes in Saccharomyces fragilis and S. cerevisiae. The conditions for eluting these enzymes from both organisms were compared. Either KCl or beta-mercaptoethanol eluted the enzymes from S. fragilis, and the amounts eluted varied quantitatively according to the physiological age of the organism. In addition to eluting enzymatic activity from the cells, these reagents also caused a large increase in the amount of activity that remained associated with the cells of S. fragilis. Invertase and acid phosphatase were not removed from cells of S. cerevisiae by KCl or beta-mercaptoethanol. These enzymes were separated from S. cerevisiae cells only when there was some degree of cell-wall digestion by snail gut fluid.
D000135:Acid Phosphatase; D006026:Glycoside Hydrolases; D066298:In Vitro Techniques; D008623:Mercaptoethanol; D011189:Potassium Chloride; D012440:Saccharomyces / Q000201:enzymology*
D008623:Mercaptoethanol; D011189:Potassium Chloride; D000135:Acid Phosphatase; D006026:Glycoside Hydrolases