Relationship of a Wall-Associated Enzyme with Specific Layers of the Cell Wall of a Gram-Negative Bacterium
AUTOR(ES)
Costerton, J. W.
RESUMO
In untreated cells of the marine pseudomonad studied here, alkaline phosphatase was found to be located in the periplasmic space, at the cell surface, and in the medium into which it had been shed during growth. Washing in 0.5 M NaCl, which removed the loosely bound outer layer, caused a shift of periplasmic enzyme to the outer aspect of the double-track layer and released some of the cell surface-associated enzyme. When the double-track layer of the cell wall was partially deranged, large amounts of this cell wall-associated enzyme were released, and, when the double-track was removed from the cells to produce mureinoplasts, alkaline phosphatase was released into the menstruum. There was no significant association of the enzyme with the peptidoglycan layer of the cell wall, which is the outermost structure of the mureinoplast, and no association of the enzyme with the cytoplasmic membrane of these modified cells. This study has shown that alkaline phosphatase is specifically associated with the outer layers of the cell walls of cells of this organism and is retained within the cell wall by virtue of this association.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=285392Documentos Relacionados
- Separation and Localization of Cell Wall Layers of a Gram-Negative Bacterium
- Quantitation, Chemical Characteristics, and Ultrastructure of the Three Outer Cell Wall Layers of a Gram-Negative Bacterium
- Effect of the Removal of Outer Cell Wall Layers on the Actinomycin Susceptibility of a Gram-Negative Bacterium
- Heterogeneity and Distribution of Lipopolysaccharide in the Cell Wall of a Gram-Negative Marine Bacterium
- Demonstration by Freeze-Etching of a Single Cleavage Plane in the Cell Wall of a Gram-Negative Bacterium