General Comments on Buffers
R Lundblad
Citation
R Lundblad. General Comments on Buffers. The Internet Journal of Genomics and Proteomics. 2006 Volume 2 Number 2.
Abstract
The major factor in biological pH control in eukaryotic cells is the carbon dioxoide-biocarbonate-carbonate buffer (Scheme I) system1,2,3,4. There other biological buffers such as bulk protein and phosphate anions which can provide some buffering effect, metabolites such as lactic acid which can lower pH and tris(hydroxylmethylaminomethyl) methane, THAM®) has been used to treat acid base disorders5,6,7. pH control in prokaryotic cells is mediated by membrane transport of various ions including hydrogen, potassium and sodium8,9,10.
In the laboratory, the bicarbonate/carbonate buffer system can only be used in the far alkaline range (pH 9-11) and unless “fixed” by a suitable cation such as sodium, can be volatile.
A variety of buffers, most notably the “Good” buffers which were developed by Norman Good and colleagues[[[10a]]], have been developed over the years to provide pH control in
Other specific examples are presented in Table 1.
1. Tunnicliff, G. and Smith, J.A., Competitive inhibition of gamma-aminobutyric acid receptor binding by
2. Durham, A.C., A survey of readily available chelators for buffering calcium ion concentrations in physiological solutions,
3. Stellwagen, N.C., Bossi, A., Gelfi, C. and Righetti, P.G., DNA and buffers: Are there any noninteracting neutral pH buffers?,
4. Syvertsen, C. and McKinley-McKee, J.S., Affinity labelling of liver alcohol dehydrogenase. Effect of pH and buffers on affinity labelling with iodoacetic acid and (
5. Biyani, M. and Nishigaki, K., Sequence-specific and nonspecific mobilities of single-stranded oligonucleotides observed by changing the borate buffer concentration,
6. Zittle, Z.A., Reaction of borate with substances of biological interest,
7. Weitzman, S., Scott, V., and Keegstra, K., Analysis of glycoproteins as borate complexes by polyacrylamide gel electrophoresis,
8. Patthy, L. and Smith, E.L., Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residues,
9. Jacobson, K.B., Murphey, J.B., and Sarma, B.D., Reaction of cacodylic acid with organic thiols,
10. Cheung, S.T. and Fonda, M.L., Reaction of phenylglyoxal with arginine. The effect of buffers and pH,
10a. Good, N.E., Winget, G.D., Winter, W.,
11. Uppu, R.M., Squadrito, G.L., and Pryor, W.A., Acceleration of peroxynitrite oxidations by carbon dioxide,
12. Denicola, A., Freeman, B.A., Trujillo, M., and Radi, R., Peroxynitrite reaction with carbon dioxide/bicarbonate: kinetics and influence on peroxynitrite-mediated oxidations,
13. Munday, R., Munday, C.M. and Winterbourn, C.C., Inhibition of copper-catalyzed cysteine oxidation by nanomolar concentrations of iron salts,
14. Jansson, P.J., Del Castillo, U., Lindqvist, C., and Nordstrom, T., Effects of iron on vitamin C/copper-induced hydroxyl radical generation in bicarbonate-rich water,
15. Ramirez, D.C., Mejiba, S.E. and Mason, R.P., Copper-catalyzed protein oxidation and its modulation by carbon dioxide: enhancement of protein radicals in cells,
16. Tadolini, B., Iron autoxidation in Mops and Hepes buffers,
17. Simpson, J.A., Cheeseman, K.H., Smith, S.E., and Dean, R.T., Free-radical generation by copper ions and hydrogen peroxide. Stimulation by Hepes buffer,
18. Sokolowska, M. and Bal, W., Cu(II) complexation by "non-coordinating"
19. Bowman, C.M., Berger, E.M., Butler, E.N.
20. Magonet, E., Briffeuil, E., Polimay, Y., and Ronveaux, M.F., Adverse-effects of HEPES on human-endothelial cells in culture,
21. Mash, H.E., Chin, Y.P., Sigg, L.,
22. Altura, B.M., Carella, A., and Altura, B.T., Adverse effects of Tris, HEPES, and MOPS buffers on contractile responses of arterial and venous smooth muscle induced by prostaglandins,
23. Tadolini, B., and Sechi, A.M., Iron oxidation in Mops and Hepes buffers,
24. Schmidt, K., Pfeiffer, S., and Meyer, B., Reaction of peroxynitrite with HEPES or MOPS results in the formation of nitric oxide donors,
25. Zhao, G. and Chasteen, J.D., Oxidation of Good's buffers by hydrogen peroxide,
26. Dudley, K.H. and Bius, D.L., Buffer catalysis of the racemization reaction of some 5-phenylhydantoins and its relation to in vivo metabolism of ethotoin,
27. Lazarus, R.A., Chemical racemization of 5-benzylhydantoin,
28. Moore, S.A., Kingston, R.L., Loomes, K.M.,
29. Schmidt, J., Mangold, C., and Deitmer, J., Membrane responses evoked by organic buffers in identified leech neurones,
30. Robinson, J.D. and Davis, R.L., Buffer, pH, and ionic strength effects on the (Na+ + K+)-ATPase,
31. Poole, C.A., Reilly, H.C., and Flint, M.H., The adverse effects of HEPES, TES, and BES zwitterionic buffers on the ultrastructure of cultured chick embryo epiphyseal chondrocytes,
32. Pogány, G., Hernandez, D.J., and Vogel, K.G., The
33. Grande, H.J. and Van der Ploeg, K.R., Tricine radicals as formed in the presence of peroxide producing enzymes,
34. Oliver, R.W. and Viswanatha, T., Reaction of tris(hydroxymethyl)aminomethane with cinnamoyl imidazole and cinnamoyltrypsin,
35. Ray, T., Mills, A., and Dyson, P., Tris-dependent oxidative DNA strand scission during electrophoresis,
36. Qi, Z., Li, X., Sun, D.,