|Jmol-3D images||Image 1|
|Molar mass||121.14 g mol−1|
|Appearance||White crystalline powder|
|Melting point||>175-176 °C (448-449 K)|
|Boiling point||219 °C; 426 °F; 492 K|
|Solubility in water||~50 g/100 mL (25 °C)|
|R-phrases||R36 R37 R38|
| (what is: / ?)
Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
Tris, also known as THAM (the shorter names being abbreviations of tris(hydroxymethyl)aminomethane), is an organic compound with the formula (HOCH2)3CNH2. Tris is extensively used in biochemistry and molecular biology. In biochemistry, Tris is widely used as a component of buffer solutions, such as in TAE and TBE buffer, especially for solutions of nucleic acids. It is a primary amine and thus undergoes the reactions associated with typical amines, e.g. condensations with aldehydes.
- The pKa declines approximately 0.03 units per degree Celsius rise in temperature.
- Silver-containing single-junction pH electrodes (e.g., silver chloride electrode) are incompatible with Tris (Ag-tris precipitation clogs the junction). Double-junction electrodes are resistant to this problem, and non-silver containing electrodes are immune.
- Making buffer solutions by neutralizing TrisHCl requires attention to the attendant changes in ionic strength.
- Tris inhibits a number of enzymes, and therefore it should be used with care when studying proteins.
The useful buffer range for tris (7-9) coincides with the physiological pH typical of most living organisms. This, and its low cost, make tris one of the most common buffers in the biology/biochemistry laboratory. Tris is also used as a primary standard to standardize acid solutions for chemical analysis.
Tris is used to increase membrane permeability of cell membranes.
- Gomori, G., Preparation of Buffers for Use in Enzyme Studies. Methods Enzymology., 1, 138-146 (1955).
- El-Harakany, A.A.; Abdel Halima, F.M. and Barakat, A.O. (1984). "Dissociation constants and related thermodynamic quantities of the protonated acid form of tris-(hydroxymethyl)-aminomethane in mixtures of 2-methoxyethanol and water at different temperatures". J. Electroanal. Chem. 162 (1–2): 285–305. doi:10.1016/S0022-0728(84)80171-0.
- Vega, C.A.; Butler, R.A. et al. (1985). "Thermodynamics of the Dissociation of Protonated Tris(hydroxymethy1)aminomethane in 25 and 50 wt % 2-Propanol from 5 to 45 °C". J. Chem. Eng. Data 30 (4): 376–379. doi:10.1021/je00042a003.
- Desmarais, WT; et al. (2002). "The 1.20 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: A tale of buffer inhibition". Structure 10 (8): 1063–1072. doi:10.1016/S0969-2126(02)00810-9. PMID 12176384.
- Ghalanbor, Z; et al. (2008). "Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity". Protein Peptide Lett. 15 (2): 212–214. doi:10.2174/092986608783489616. PMID 18289113.
- Markofsky, Sheldon B. (2000). Nitro Compounds, Aliphatic. doi:10.1002/14356007.a17_401.
- Irvin, R.T.; MacAlister, T.J.; Costerton, J.W. (1981). "Tris(hydroxymethyl)aminomethane Buffer Modification of Escherichia coli Outer Membrane Permeability". J. Bacteriol 145 (3): 1397–1403.
- Kallet, RH; Jasmer RM, Luce JM et al. (2000). "The treatment of acidosis in acute lung injury with tris-hydroxymethyl aminomethane (THAM)". American Journal of Respiratory and Critical Care Medicine 161 (4): 1149–1153. PMID 10764304.