Triethanolamine buffer

Calcium. 25.0 mL calcium ion solution + 25 mL ammonia or triethanolamine buffer. 

The concentration of hydroxypyruvate was determined by spectrophotometry at 340 nm. A 20 pL aliquot from the reaction mixture was introduced into 1 mL of triethanolamine buffer (0.1 m) at pH 7.6 containing 20 /rL of NADH solution in water (14 mm, 0.28 /imol) and 2 units of L-lactate dehydrogenase. The absorbance due to NADH is proportional to the concentration of hydroxypyruvate. 

Prepare serum by ammonium sulfate precipitation (45% saturation). Redissolve the precipitate m 0.02M triethanolamine buffer, pH 7 7, and dialyze overnight against this buffer at 4°C Filter (0.2 pm) the sample before use (see Note 8). 

Equilibrate the column with 0 02M triethanolamine buffer, pH 7.7 (buffer A) Run a blank gradient from 0-100% buffer B (buffer A + 1M NaCl). Use a flow rate of 4-6 mL/min for this and subsequent steps. 

Triethanolamine buffer 0.02M triethanolamine, pH 7.7. For ionic gradient separations by fast-protein liquid chromatography (FPLC), also use triethanolamine buffer containing IMNaCl. Store at 4°C. 

The method involves initial leaching of the soil with a solution of barium chloride-triethanolamine buffered at pH 8.1, followed by calcium saturation. The Ca-saturated soil is equilibrated with standard phosphoric acid solution and the quantity of phosphorus adsorbed is evaluated. From this adsorbed phosphorus plus phosphorus extracted initially the AEG of the soil is calculated using the formula. 

E3 UDP-sugar phosphorylase. E4 pyrophosphatase. (Below) Synthesis of 6 -deoxy-6 -fluorosucrose. El, sucrose synthetase E2, pyruvate kinase E3, UDP-glucose pyrophosphorylase E4, pyrophosphatase. All enzymes (150 U each) are co-immobilized in polyacrylamide gel. The reactions are carried out in triethanolamine buffer (50 mM) containing MgCl2 (10 mM) with pH being controlled at 7.5 by addition of IN NaOH. The 500-mL reaction mixture contains glucose-... 

Frequently used buffers are acetate, phosphate, Tris, triethanolamine, HEPES, PIPES, and MOPS. The pKa of acetate and phosphate buffers is independent of the temperature. This advantage comes with the disadvantage of the narrow range of acetate buffers (pH 4.5 to 5.5) and of the tendency of phosphate to fall out of solution with divalent cations. The pKa of Tris and triethanolamine buffers is highly temperature dependent. 

Prehybridization steps are identical for tissue hybridized with the [ S]-radi-olabeled probe alone and tissue hybridized with the digoxigenin-labeled ribo-probe apphed in combination with the appropriate [ S]-radiolabeled probe. Slides are allowed to equilibrate to room temperature, are loaded into slide racks, fixed in formaldehyde-PBS buffer, rinsed in triethanolamine buffer (TEA-HCl), and incubated in TEA-HCl with fresh acetic anhydride added (10 min). Slides are subsequently dehydrated in ascending concentrations of ethanol, defatted by incubation in chloroform, rinsed in ethanol and air-dried. At this point, slides are now ready to be hybridized, although slides can also be stored at -80°C without loss of signal. 

Providing the pH value is above 5.5, there is no interference from hydrogen ions. In this respect, the pH of venous blood is of the order of 7.3—7.4, but the buffering effect of carbon dioxide can cause difficulties — a loss apparently causing a decrease and a gain an increase in ionic calcium, respectively [53]. This also calls for caution in the use of buffers unless their effects on calcium ionic activity is known. Some authors have added trypsin and triethanolamine buffer to their ionised calcium standards [3j. 

Trypsin and triethanolamine buffer in ionised calcium standards are said to decrease equilibration time and to lead to better electrode reproducibility [3,59,86] and the serum data corresponding to references 59, 79 and 102 in Table 2.3 refer to electrodes calibrated with such buffers added to the usual calcium chloride standards containing 0.150 mol dm sodium chloride. However, such buffered standards must be prepared immediately before use with highly purified trypsin and filtered immediately so as to remove undissolved trypsin [55,59,80]. 

Figure 20. Time courses of hydrogen consumption rate and catalyst potential during hydrogenation on suspended catalyst at 298 K (Beck ° ). (lA, B) Hydrogenation of dimethylethinyl carbinol on Pd (4.5%)/Si02 catalyst (5 g). 0,5 M in triethanolamine-buffered methanol solution (pH 8), 500 cm (2A, B) Hydrogenation of 2-butyne-l,4 diol on Pd (5%)/Al203 catalyst (5 g). 0.06 M solution in triethanolamine buffered aqueous solution (pH 8), 500 cm. ...

FIGURE 11 Reciprocal of response time, l/Tj jr versus buffer concentration for an electrode array coated with an 80 20 HEMArDMA hydrogel and tested in phosphate buffer (1, 5, 10, 25. 50, and 100 mM) and triethanolamine buffer (5, 25, and 50 mM). Symbols represent characteristic response times for (o) a pH increase from 7.2 to 7.4 in phosphate buffer ( ) a pH decrea.se from 7.4 to 7.2 in phosphate ( ) a pH increase from 7.2 to 7.4 in triethanolamine buffer ( ) a pH decrease from 7.4 to 7.2 in triethanolamine buffer. Standard errors are shown. The solid lines represent linear regressions of the data. 

FIGURE 12 Dependence of on pH-p fp for an electrode array coated with an 80 20 HEMA DMA hydrogel and tested in 100 mM phosphate and 100 mM triethanolamine buffer. Symbols represent characteristic response times for ( ) a device responding to pH increases of 0.20, 0.32, 0.40, and 0.57 pH unit in phosphate buffer ( ) a device responding to pH increases of 0.20, 0.33, 0.44, and 0.60 pH unit in triethanolamine buffer. The solid curves represent the theoretical characteristic response time replotted from Fig. 2b (shaded area) and calculated from Eq. 4. 

Zero spectrophotomenter against distilled water, check zero at frequent intervals throughout experiment. Pipette 3 ml of triethanolamine buffer at 20-25 °C into a... 

The enzyme is available at a omcentiation of 10 mg/ml in 30 mM triethanolamine buffer pH 7.6. (This buffer does not interfiere with the labelling reaction.)... 

Just before use, dilute acetic anhydride to 0.25% v/v in 0.1 M triethanolamine buffer. Mix vigorously and immediately immerse the slides in this solution Incubate for 10 min while occasionally moving the slide rack up and down. 

The sensitivity of semicarbazone derivatization in PLP and PL analysis is illustrated by the application of HPLC to study vitamin Be metabolism in human lymphocytes. Lymphocytes were isolated from 10 mL of blood 5 pL of packed lymphocytes was diluted to 100 pL using a 10-mM triethanolamine buffer (pH 7.4) containing 0.1% Triton X-100. After homogenization (MSB ultrasound ho-mogenizer), 60 pL of the homogenized suspension was diluted to 400 pL in buffer A (10 mmol/L triethanolamine, 90 mmol/L K2HPO4, 2 mmol/L MgCl 2, 2.6 mmol/L ATP pH 7.4). To a 100-pL aliquot, 50 pL of 10% trichloroacetic... 

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