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Tris propane

Bis(2-methoxyethoxy)ethane, t282 Bis-tris propane, b237... [Pg.115]

N-(2-Acetamido)-2-aminoethane-sulfonic acid (ACES ) 1,3-Bis[tris(hydroxymethyl)-methylaminolpropane (BIS-TRIS PROPANE) 3-(N-Morpholino)-2-hydroxy-propanesulfonic acid (MOPSO)... [Pg.323]

BlS-Tris propane (1.3-bis[tris (hydroxymethyl)-methylamino] propane) (pK2)... [Pg.194]

Why should l-[tris propan-2-yl) ilyl]pyrrole react with jV-bro-mosuixinimide (a source of Br,) to give 3-bromo-l-[tris(propan-2-yt)silyl]pyrrole, rather than the 2-isomer ... [Pg.95]

The kinetics of the hydrolysis of di(2,4-dinitrophenyl) phosphate (DDNPP) were studied in basic solutions buffered with Bis-Tris propane (BTP) in the presence of La3+, Sm3+, Tb3+, and Er3+. Two equivalents of the 2,4-dinitrophenolate ion were liberated for each equivalent of DDNPP and the reaction showed first-order kinetics. Potentiometric titrations showed the formation of dinuclear complexes such as [Ln2(BTP)2(OH) ](6 " i, with values of n varying as a function of pH for all studied metals. Hence the catalytic effect depends on the formation of dinuclear lanthanide ion complexes with several hydroxo ligands.97... [Pg.76]

Data presented as KIE Arrhenius plots (see explanation and description under Methods). All the experiments were carried out in lOmM bis-tris propane buffer pH 9.0 as described under Methods. [Pg.316]

Determination of enthalpy of activation requires measurements of kcat under full substrate saturation over a significant temperature range. The initial velocity measurements were performed under pure oxygen atmosphere and with 0.5 M 2-deoxyglucose (> 8 Km) in 10 mM bis-tris propane buffer pH 9 as described under... [Pg.317]

Lysine-labelled tryptophanase was prepared by Incubating the enzyme with 100-fold molar excess of 2,2,5,5-tetramethyl-3-pyrrolin-1-oxyl-3-carboxylic acid N-hydroxysuccinimide ester (Eastman Kodak Company) in 10 mM bis-tris-propane (Sigma), pH 8 (20% v/v... [Pg.111]

Co(H2N—CH2—CH(CH3)—NH2)3](C104)3 tris(propane-l,2-diamine)cobalt(III) perchlorate... [Pg.274]

Figure 6-7 Cyclic voltammograms on a 4,4 -dithiodipyridme modified gold electrode of a 200 pM P. denitrificans CCP solution in lOOmM bis-tris-propane, lOOmM KNO3, pH 6.3. Panel A High potential region. Panel B Low potential region. (1) Calcium loaded CCP (incubated with ImM Ca ) (2) Calcium depleted CCP (EDTA treated). Scan rate, 20mVs , temperature, 22+1 °C. The potential axis is defined versus the normal hydrogen electrode (NHE) (adapted from [22]). Figure 6-7 Cyclic voltammograms on a 4,4 -dithiodipyridme modified gold electrode of a 200 pM P. denitrificans CCP solution in lOOmM bis-tris-propane, lOOmM KNO3, pH 6.3. Panel A High potential region. Panel B Low potential region. (1) Calcium loaded CCP (incubated with ImM Ca ) (2) Calcium depleted CCP (EDTA treated). Scan rate, 20mVs , temperature, 22+1 °C. The potential axis is defined versus the normal hydrogen electrode (NHE) (adapted from [22]).
BIS TRIS PROPANE I,3-5is[tris(hydroxymethyI)methyIamino]propane 282.3 6.8 6.3—9.5... [Pg.1187]

After each activity measurement, the nanoencapsulated-enzyme samples were transferred with a pipet from the reaction vessel back to a centrifuge tube for reusability analyses. The samples were centrifuge washed, as described earlier, for three times, in 10 mM bis-tris propane, pH 7.2, and the supernatant was decanted and retained for analysis of enzyme leakage. The final washed sample was then stored, decanted dry, in its tube at 6 C until next trial. [Pg.239]

Figure 1, Percent relative enzymatic activity of the nanoencapsulated preparation gelation time to free OPAA in 50 mMbis-tris propane, pH 8. The nanoencapsulated preparation contained TMOS + KH MS + OPAA. The activity was measured at initial mixture (Gl = 0 min), 15 min later (G2 = 15 min), and 30 min later (G3 = 30 min). Standard condition was 50 mM bis-tris propane, pH 8. Free enzyme in standard condition is 1013 U/mg. Figure 1, Percent relative enzymatic activity of the nanoencapsulated preparation gelation time to free OPAA in 50 mMbis-tris propane, pH 8. The nanoencapsulated preparation contained TMOS + KH MS + OPAA. The activity was measured at initial mixture (Gl = 0 min), 15 min later (G2 = 15 min), and 30 min later (G3 = 30 min). Standard condition was 50 mM bis-tris propane, pH 8. Free enzyme in standard condition is 1013 U/mg.
Figure 2. Comparison of the nanoencapsulated OPAA activity in different solvents relative to free OPAA in 50 mM bis-tris propane, pH 8. The nanoencapsulated OPAA samples were TMOS-F50-OPAA, TMOS-PEG-OPAA, MTMS-PEG-OPAA, 3MTMS-F50-OPAA, 3MTMS-wet gel, 3MTMS-OPAA, and MTMS-OPAA. The solvents studied were 20% hexane (vertical bars), 20% acetone (shaded bars), 20% methanol (horizontal bars), 20% dimethyl-formamide (unshaded bars), and control buffer, 50 mMbis-tris propane (diagonal bars). The activity of free OPAA in 50 mMbis-tris propane, pH 8... Figure 2. Comparison of the nanoencapsulated OPAA activity in different solvents relative to free OPAA in 50 mM bis-tris propane, pH 8. The nanoencapsulated OPAA samples were TMOS-F50-OPAA, TMOS-PEG-OPAA, MTMS-PEG-OPAA, 3MTMS-F50-OPAA, 3MTMS-wet gel, 3MTMS-OPAA, and MTMS-OPAA. The solvents studied were 20% hexane (vertical bars), 20% acetone (shaded bars), 20% methanol (horizontal bars), 20% dimethyl-formamide (unshaded bars), and control buffer, 50 mMbis-tris propane (diagonal bars). The activity of free OPAA in 50 mMbis-tris propane, pH 8...

See other pages where Tris propane is mentioned: [Pg.162]    [Pg.937]    [Pg.151]    [Pg.1206]    [Pg.180]    [Pg.225]    [Pg.235]    [Pg.193]    [Pg.126]    [Pg.174]    [Pg.175]    [Pg.129]    [Pg.180]    [Pg.239]    [Pg.35]    [Pg.174]    [Pg.312]    [Pg.314]    [Pg.178]    [Pg.92]    [Pg.162]    [Pg.156]    [Pg.1157]    [Pg.223]    [Pg.223]    [Pg.1138]    [Pg.50]    [Pg.1193]    [Pg.3280]    [Pg.5268]    [Pg.236]    [Pg.237]    [Pg.237]    [Pg.241]    [Pg.243]    [Pg.243]    [Pg.247]   
See also in sourсe #XX -- [ Pg.153 ]

See also in sourсe #XX -- [ Pg.187 ]




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