The Journal of Pathology and Bacteriology · 1966 · 51 citations · 1 references
Life SciencesBiochemistryMicrobiologyCellular MetabolismEnzymologyMetabolismNon-saccharomyces YeastsYeast BiologyDigestionEnzymesInvertase ActivityYeast MetabolismYeast-substrate Interactions
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 KCI or ,3-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 KCI or ,B-mercaptoethanol. These enzymes were separated from S. cerevisiae cells only when there was some degree of cell-wall digestion by snail gut fluid.
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Prevention of Coprophagy in the Rat
Richard H. Barnes, Grace Fiala, Bette McGehee et al. · Journal of Nutrition · 1957 · 123 citations
Veterinary Medicine, Veterinary Parasitology, Pathophysiology +3