El-Harakany, A.A.; Abdel Halima, F.M. and Barakat, A.O. 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 (англ.) // J. Electroanal. Chem.[англ.] : journal. — 1984. — Vol. 162, no. 1—2. — P. 285—305. — doi:10.1016/S0022-0728(84)80171-0.
Vega, C.A.; Butler, R.A. et al. Thermodynamics of the Dissociation of Protonated Tris(hydroxymethy1)aminomethane in 25 and 50 wt % 2-Propanol from 5 to 45 °C (англ.) // J. Chem. Eng. Data : journal. — 1985. — Vol. 30. — P. 376—379. — doi:10.1021/je00042a003.
Desmarais, WT; et al. The 1.20 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: A tale of buffer inhibition (англ.) // Structure : journal. — 2002. — Vol. 10, no. 8. — P. 1063—1072. — doi:10.1016/S0969-2126(02)00810-9. — PMID12176384.
Ghalanbor, Z; et al. Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity. (англ.) // Protein Peptide Lett. : journal. — 2008. — Vol. 15, no. 2. — P. 212—214. — doi:10.2174/092986608783489616. — PMID18289113.
Desmarais, WT; et al. The 1.20 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: A tale of buffer inhibition (англ.) // Structure : journal. — 2002. — Vol. 10, no. 8. — P. 1063—1072. — doi:10.1016/S0969-2126(02)00810-9. — PMID12176384.
Ghalanbor, Z; et al. Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity. (англ.) // Protein Peptide Lett. : journal. — 2008. — Vol. 15, no. 2. — P. 212—214. — doi:10.2174/092986608783489616. — PMID18289113.
El-Harakany, A.A.; Abdel Halima, F.M. and Barakat, A.O. 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 (англ.) // J. Electroanal. Chem.[англ.] : journal. — 1984. — Vol. 162, no. 1—2. — P. 285—305. — doi:10.1016/S0022-0728(84)80171-0.
