Tris

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Tris

Abbreviation for tris(hydroxymethyl)aminomethane and tris(hydroxymethyl)methylamine; a buffer; used as a trivial name.
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The sections were washed with distilled water, then again dipped in Tris buffer solution.
Aedes albopictus [PLA.sub.2] activity was significantly higher in the buffer containing EGTA (M = 0.063, SEM = 0.01) and Tris buffer (M = 0.065, SEM = 0.00), while, for Culex quinquefasciatus, the [PLA.sub.2] activity was significantly high in Tris buffer (M = 0.089, SEM = 0.01) compared to enzyme activity in Tris buffer with additional calcium (M = 0.0087, SEM = 0.01) (Figure 2).
The NSNCs were stable in Tris buffer and media serum with no sign of precipitation.
Absorbance measurements were made on the TRIS buffer, tryptophan solution, and uracil solution using the calibrated short-pathlength cuvettes on the Cary transfer spectrophotometer.
Active Fraction (22-30) was obtained from Sephadex G-100 column chromatography while contained (8.8mg protein) was lyophilized and dissolved in 1 ml of 0.1 M tris buffer then applied to the top of DEAE Sephadex-A52 column chromatography (35 cm x 2.5 cm) previously equilibrated with 0.1 M tris buffer at pH 7.0 at 11 C.
First, each material based on mix proportion specified as shown in Table 1 was prepared and they were mixed with Tris buffer solution in a beaker.
Protein samples of 1 mg/ml, HSA or GHSA+DTT 3.4 mM dissolved in Tris buffer (50 mM, pH=7.4), with or without additives (Alg, [beta]-CyD or Tre), were prepared.
Control reactions were incubated with Tris buffer without meprins.
Calcium In Tris Buffer, AGZN0 showed more prominent release of calcium with time (Fig 1) whereas in AA, cal- cium release was lower as compared to zinc containing batches (Fig 2).
The intrins ic fluores cence intens ity of DNA is very lo w and that of EB in Tris buffer is als o not high due to quenching by the solvent molecu les .
The partially purified AChE displayed the highest activity on ATC at pH 7 and at 30oC using 0.1 M Tris buffer. The enzyme exhibited Michaelis-Menten kinetic constants, Km, for ATC, BTC and PTC at 36, 77 and 250 M, respectively, and the maximum velocities, Vmax, were 18.75, 0.12 and 0.05 mol/min/mg protein, respectively.
The solution was loaded onto a DEAE-Sepharose Fast Flow column (GE Healthcare) equilibrated with Tris buffer (pH 9.0, ionic strength = 10 mM, 50 mM Tris and 4.3 mM NaCl) and eluted with a linear gradient of Tris buffer (pH 9.0, ionic strength = 10 mM, 50 mM Tris and 4.3 mM NaCl), -1 M NaCl.