Characterization of the glycolysis pathway and the plasma membrane of Lactobacillus and Bifidobacterium strains.
The characteristics of the glycolytic pathway and the plasma membrane of Lactobacillus and Bifidobacterium were studied. The enzyme system of glycolysis (hexokinase, glucokinase and pyruvate kinase) which is the main source of energy in the anaerobic condition was localized in the cell soluble fraction (cytoplasma) of all species examined. Neither electron transfer chain components nor oxidase activities were found in anaerobically cultured Lactobacillus and Bifidobacterium. Adenosine triphosphatase (ATPase) activities were mainly localized in the plasma membrane, suggesting that membrane ATPase is playing a key role in membrane transport and ATP synthesis of anaerobic bacilla. SDS-polyacrylamide gel electrophoresis of membranes showed remarkable differences between the polypeptides patterns of B. adolescentis and B. bifidum. Such peculiarities in polypeptide patterns among the same genus may be useful in the identification of species.
D000251:Adenosine Triphosphatases / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology; D005941:Glucokinase / Q000032:analysis; D006019:Glycolysis; D006593:Hexokinase / Q000032:analysis; D007778:Lactobacillus / Q000201:enzymology*
D006593:Hexokinase; D005941:Glucokinase; D000251:Adenosine Triphosphatases