TMA buffer

Fig. 8. Salt dependence of enzyme synthesis in an S30 system. (Experiment together with H. J. Rahmsdorf.) 50 ml of an exponentially growing culture of strain XA 7007 (suA) in rich medium were harvested at O.D.goo = 0.4. After washing once with TMA buffer, the cells were suspended in 0.4 ml TMA buffer and lysed by ultrasonication. The debris were removed. The S30 incubation mixture contained, in addition to 20 (d of the S30 extract, the following components in a final volume of 0.05 ml tris HCl pH 8.0 51 mM K-acetate 50 mM amino acids 0.2 mM each ATP 2mM UTP, CTP, GTP 0.5 mM each PEP 20 mM dithiothreitol 2.5 mM tRNA 500 (xg/ml T3 DNA 50 xg/ml MgClg 11 mM (the S30 extract adds to 15 mM MgClg in toto) varying concentrations of NH4CI. After 40 minutes at 37°, aliquots were tested for lysozyme (o-------o)...

Fig. 15. Dependence of T3 DNA directed SAMase synthesis on Mg + and Mn + concentration. SAMase synthesis was performed in the DEAE system as described in Table 2. Synthesis was allowed to proceed at various concentrations of MgClg or MnClg. In the cases of manganese addition a basal concentration of 5 mM MgClj.was present in all samples because the system itself had been prepared with TMA buffer...

Recombinant protein in acetate buffer, spiked with 10 pg/ml TEA, TMA and... 

Figure 12.1 Clearance of small-molecule impurities from process buffers in a formulated protein product. Trace A the NMR spectrum of a control sample containing a mixture of three components (succinate, tetraethylammonium, and tetramethylammonium) in the final formulation buffer (sodium acetate). These three components were used in the recovery process for a biopharmaceutical product. Traces B and D the proton NMR spectra of the formulated protein product. No TEA or TMA were detected, but a small amount of succinate was observed in this sample. Traces C and E the proton NMR spectra of a formulated protein product spiked with 10 jag/ml of succinate, TEA, and TMA. Traces D and E were recorded with CPMG spin-echo method to reduce the protein signals. The reduction of NMR signals from the protein allows for better observation of the small-molecule signals.

A review by Galli et al. describes several buffer-absorbing chromophores as co-ions. These include phthalate, PDG (2,6-pyridinedicarboxylic acid), PMA (1,2,4,5-benzenetetra-carboxylic acid or pyromellitic acid), TMA (trimellitic acid), MES, 2,4-dihydrobenzoic acid with s-aminocaproic acid, p-hydroxybenzoate, p-anisate, 3,5-dinitrobenzoic acid, salicylic acid with TRIS, benzoic acid with tris (hydroxymethyl)aminomethane (TRIS), and many others. On the other hand, some inorganic chromophores such as chromate (Figure 9) or molybdate may be added to a buffer. A BGE-containing chromate should have a pH above 8, because it precipitates below this value. The advantage of a TRIS buffer or buffers at around pH 6 is that carbonate will not interfere with the separation because it is not soluble in TRIS or at lower pHs. 

Figure 2. Electron paramagnetic resonance spectra of Mr bound to the single catalytic site on (Na + K )-ATPase. The X-hand spectrum (9.5 GHz) is shown in A, while the K-band spectrum (35 GHz) of the same complex is shown in B. The enzyme-Mn2 complex was centrifuged out of 20mM Tes-TMA, pH 7.5, and then combined with buffer so that the final concentrations were 0.15mM (Ha 4-K )-A TPase, 0.1 mM MnCl, 20mM Tes-TMA, pH 7.5. T = 23°C.

Figure 12. Titration of GdCl with Ca2 -ATPase (24). The solutions contained 0.05M TMA-Pipes buffer, pH 7.0, 24.4 pM GdCl, (A) or 49pM GdCl, (B), and the noted concentrations of Ca2 -ATPase. The value of t obtained by extrapolation of the solid line to the infinite protein concentration is the average of the enhancements at Gd3 sites 1 and 2, denoted by c , and iBi, respectively, in the text.

The NMR experiments were undertaken on 28 mM (in nucleotides) poly(dA-dT) in 10 mM cacodylate buffer, to which 1 M salt solutions were added. The samples contained in addition 1 mM and 10 mM EDTA for the proton and phosphorus NMR studies, respectively. The experimental conditions are indicated in order to emphasize that even in 1 M TMA+ solutions there are Na+ ions associated with poly(dA-dT), the 10 mM buffer and the EDTA solutions. 

Photosystem II preparations isolated as per (15) oxidized water at rates of 700-850 pmol 02/mg Chi hr. The rate of O2 evolution was measured with a Clark-type electrode in a reaction mixture that contained 500 pM DCBQ, 400 mM sucrose and 50 mM MES buffered to pH 6.5 with TMA-OH. The concentration of Q" in the assay was held constant at 30 mM by the addition of TMA-Cl. Additions of Ca ", Sr and/or Na" to the assay were made from stock solutions prepared by buffering MES to pH 6.5 with Ca(OH)2, Sr(OH)2 and NaOH, respectively. 

Ming Li and Sang Hak Lee have reported a CE system integrated with ECL method in the absence of an electric field decoupler for the determination of tri-methylamine (TMA) in fish. ECL from the reaction of analyte and in sim generated Ru(bpy)3 at electrode surface could be produced in the presence of TMA. For ECL detection, a Pt working electrode biased at 1.23 V (vs. Ag/AgCl) potential was employed in a 10 mmol L sodium borate buffer solution, pH 9.2,... 

The formation process for long metallic nanoarrays with DNA nanofibers is illustrated in Fig. 5.16 [80, 109]. First, a mixture of Phenaz-TMA/AuNPs and A-DNA in a TE buffer (pH = 8) solution was added to 8 i,L of ethanol. This solution was then deposited on a PDMS sheet, which was tilted at 15° during solvent evaporation to move the drying front downwards. Solvent evaporation leads to a decrease in the volume of the solution, leaving behind line patterns. Line patterns of metallic nanoarrays were formed when DNA with AuNPs attached was continuously deposited at the highly concentrated finger positions. Metallic nanoarrays also exceed several hundred micrometers in length and can be made within 30 min. 

---