Tris(hydroxymethyl)aminomethane buffer modification of Escherichia coli outer membrane permeability

Abstract

The effect of tris(hydroxymethyl)aminomethane (Tris) buffer on outer membrane permeability was examined in a smooth strain (D280) and in a heptose-deficient lipopolysaccharide strain (F515) of Escherichia coli O8. Tris buffer (pH 8.00) was found to increase outer membrane permeability on the basis of an increased Vo of whole-cell alkaline phosphatase activity and on the basis of sensitivity to lysozyme and altered localization pattern of alkaline phosphatase. The Tris buffer-mediated increase in outer membrane permeability was found to be dependent upon the extent of exposure to and concentration of the Tris buffer. The Tris buffer effects were demonstrated not to be due to allosteric activation of cell-associated alkaline phosphatase and were specific for Tris buffer. Exposure of cells to Tris resulted in the release of a limited amount of cell envelope component. Investigators utilizing Tris buffer are cautioned that Tris is not physiologically inert and that it may interact with the system under investigation.

Evaluation of cell disruption effects on primary recovery of antibody fragments using microscale bioprocessing techniques

“…Tris is known to alter the outer membrane permeability of E. coli cells resulting in a limited release of components from the cell envelope 32. On the other hand, EDTA treatments have been reported to alter cell surface properties by changing the morphological structure of the outer membrane surface, releasing polyliposaccharides and increasing envelope permeability 33.…”

Tris buffer improves fluorescence yield of ram spermatozoa when evaluating membrane integrity

“…The underlying causes of all these effects are unclear. TRIS is not physiologically inert and may have the following effects on cells: (i) the aliphatic amino group of TRIS is chemically reactive, making it unsuitable for use in cellular systems as it is toxic to many mammalian cells (Good et al,1966); (ii) TRIS interacts with metal ions (Hanlon et al,1966), and this interferes with the calcium uptake by the membrane vesicles and cells (Upreti et al,1995); (iii) TRIS buffer inhibits the respiratory enzymes in the mitochondria (Hayashi et al,1981); and (iv) an increase in membrane permeability after exposition to TRIS has been demonstrated in E. coli (Irvin et al,1981). Some of these effects could also explain the modifications induced by this buffer on sperm motility and FI.…”

Arginine‐enveloped virus inactivation and potential mechanisms

“…115 Similarly, in strains of Escherichia coli, Tris buffer increased membrane permeability, leading to a loss of cell membrane components. 116 On the contrary to the above studies, in supported lipid bilayers, atomic force microscopy measurements demonstrated that Tris buffer reduced membrane stress, while other ions, such as Ca 2+ , increased membrane stress. 117 Though there are mixed results on the effects to lipid bilayers, Tris buffer does interact with membranes.…”

“…Tris buffer disorders and disassembles the lipid bilayer. 115,116 However, Tris buffer has also been shown to increase membrane stability. 117 Considering all inactivation factors that disrupt the lipid bilayer, it is likely that the synergistic inactivation mechanisms of arginine involve the viral membrane.…”