The lipolytic activities of the isolated cell envelope fracttions of Baker's yeast.
1. The existence of phospholipase and lipase activities in the isolated cell envelopes of baker's yeast was demonstrated. 2. The content of phospholipase was found to be markedly higher than that of lipase. 3. After partial enzymic digestion of the isolated cell envelopes, the bulk of the lipolytic activities was recovered in the sedimentable preparations, which consisted of the fragments of the plasma membrane. 4. During repeated washings, the lipase was completely released from the cell envelopes, as were also the bulk of the lipid components and most of the Mg(2+)-dependent adenosine triphosphatase, an enzyme connected with the plasma membrane. The phospholipase was more firmly bound to the preparation but not so firmly as the external saccharase. 5. These results indicate that the lipolytic enzymes found in the cell envelopes are mostly located in the plasma membrane.
D000251:Adenosine Triphosphatases / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology*; D008049:Lipase / Q000032:analysis*; D010740:Phospholipases / Q000032:analysis*; D012440:Saccharomyces / Q000201:enzymology*; D013393:Sucrase / Q000032:analysis
D010740:Phospholipases; D008049:Lipase; D013393:Sucrase; D000251:Adenosine Triphosphatases