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Buffers indicators

Metal Titration type pH Buffer Indicator (Note 1) Colour change (Note 2) Notes... [Pg.329]

The stability of some prodrugs and mutual prodrugs (8.137 and 8.139, Fig. 13) in human and rat plasma was also examined [175], An approximately tenfold acceleration was noted for the mutual prodrug 8.139 at pH 7.4 and 37° for human plasma (71/2 ca. 45 s) compared to buffer (t1/2 ca. 400 s). This and other evidence indicated that cleavage of these carbamates is enzymatic. In contrast, the A-(2-hydroxyphenyl)carbamates (8.137, Fig. 13) showed two- to threefold increases in t1/2 values in human and rat plasma compared to buffer, indicating the absence of an enzymatic hydrolysis, and modest stabilization due to binding to plasma proteins. [Pg.505]

Alkaline earths Distribution coefficients for Sr(II) and Ba(II) as a function of concentration of Ca(II) are summarized in Figures 13a and 13b. The loadings in the case of Sr(It) (Figure 2) are in the linear isotherm range or only slightly out of it. Slopes of log D vs log calcium concentration are close to the ideal value, -1. Invariance of between 0.01 M and 0.1 M acetate buffer indicates that there is no interference from acetate complexing. At the same Ca(II) concentration, is a factor of... [Pg.318]

The secondary, peroxidase-coupled antispecies antibody is diluted 1.200-1.2000 in the buffer indicated in Table 1... [Pg.219]

Amino acids are sometimes used as buffers. Indicate the appropriate pH value (s) of buffers containing aspartic acid, histidine, and serine. [Pg.69]

The half-life in diluted human serum was the same or longerthan in phosphate buffer, indicating that it is unlikely that an enzyme-catalyzed reaction occurs to release the parent drug. Indeed, the authors observed a longer half-life as the serum content was increased, which they believed was indicative of serum protein binding, affording protection from hydrolysis. [Pg.452]

FIGU RE 5.5 NMR spectrum illustrating the influence of pH on product distribution of the two types of bishydroxylamine complexes of vanadate. Conditions for the experiments 3.0 mM total vanadate, 5.0 mM total hydroxylamine, 1.0 M KC1, 20 mM HEPES buffer, indicated pH. [Pg.92]

Potential of non-specific binding (NSB) to filter membrane or plastic devices. Low recovery from either protein-filtrate or buffer indicates adsorptive losses and/or membrane rejection... [Pg.479]

Buffered Indicator Solution Prepare a mixture consisting of 700 mL of 0.1 M citric acid (anhydrous, reagent grade), 200 mL of 0.2 M disodium phosphate, and 50 mL each of 0.2% bromophenol blue and of 0.2% bromocresol green in spectrograde methanol. [Pg.115]

Procedure Dissolve 160 g of anhydrous, reagent-grade citric acid in 320 mL of water, and divide the solution equally between two 250-mL separators, 5) and S2. Add 5 mL of No-Indicator Buffer Solution to S. Add 2.0 mL of Standard Amine Solution and 5 mL of Buffered Indicator Solution to S2. Divide the Sample Solution equally between two additional 250-mL separators, S2 and S4. Add 5 mL of No-Indicator Buffer Solution to S3, and 5 mL of Buffered Indicator Solution to S4. [Pg.115]

The adsorption curve of DNA-conjugated TA-polyallylamine in pH 8.0 equilibration buffer indicated that the surface plasmon resonance (SPR) response was only slightly reversed by washing with buffer (Fig. 6A, curve I). [Pg.97]

It is clear that these relatively simple organic molecules can prevent the intermolecular cross-linking of collagen. The increased solubility in neutral salt solution as well as in acid buffers indicates that intramolecular cross-linking may also be prevented. This has been confirmed by studies of the a- and /3-components of lathyritic collagen. [Pg.119]

The fact that carbohydrates of different molecular sizes [for example, pentoses and hexoses (see Table I)] may have identical Mg values on subjection to zone electrophoresis (in borate buffers) indicates that this system cannot be used for determining the molecular size of a carbohydrate. It has been emphasized at several points in this Chapter that the most potent use for zone electrophoresis of carbohydrates in borate buffers is after mixtures of carbohydrates have been resolved into groups of similar molecular size by chromatographic procedures. [Pg.107]

Qualitative detection of excess protein in urine is largely based on use of dipstick tests. The reactive portion of the stick is coated with a buffered indicator that develops color in the presence of protein. A typical example is Albustix (Bayer Corporation, Diagnostics Division, Tarrytown, NY), in which bromphenoi blue, buffered to pH 3 with citrate, is present mostly in the protonated, yellow form. When protein is added, the affinity of the anionic form of the indicator dye for protein causes a shift of the equilibrium between anionic and protonated forms of the indicator toward formation of the blue anionic species. The intensity of the shade of blue produced is then proportional to the concentration of protein in the specimen. Combur 8 strips (Roche Diagnostics, Inc., Indianapolis, IN) are said to be less subject to drug interferences. Their detection hmit is 7mg/dL. [Pg.576]

The Streptomyces PLD consists of two highly interacting components of similar topology [13]. Overall, the structure is very similar to die Nuc dimer. Each component consists of a /1-sheet of 8-9 strands surrounded by nine a-helices. The catalytic center is also very similar to that of the Nuc dimer. Crystallization with a phosphate buffer indicates that the phosphate head group of the substrate lies in contact with His, Lys and Asn residues contributed from both HKD domains [13]. [Pg.57]

For the systems described in 8.1, draw sharpness and buffer indices. [Pg.174]

A state machine representing the address interface is extracted from the Green description. This contains only the states of the buffers indicated above. The outputs MemOut and Throw are also modelled as buffers that immediately empty. [Pg.141]

Fig. 4 - An optic fiber biosensor for cocaine using a mAb against benzoylecgonine as the biological sensing element, (left) The time course of binding of FL-BE to the mAb-coated fiber expressed by the fluorescent signal transmitted via the fiber. After reaching steady state, FL-BE was withdrawn from the flow buffer (indicated by the arrow). The bound FL-BE dissociated and fluorescence decreased exponentially, (right) Reusability of the biosensor for multiple assays of cocaine introduced into the flow buffer after steady-state fluorescence (200 mV) was achieved. Cocaine at the indicated concentrations was added to the flow buffer for only the time intervals indicated by the bars. The downward deflection resulted from displacement of FL-BE by cocaine, but upon removal of cocaine from the flow buffer FL-BE displaced the bound cocaine. Reproduced with permission from reference 4, Copyright 1995 American Chemical Society. Fig. 4 - An optic fiber biosensor for cocaine using a mAb against benzoylecgonine as the biological sensing element, (left) The time course of binding of FL-BE to the mAb-coated fiber expressed by the fluorescent signal transmitted via the fiber. After reaching steady state, FL-BE was withdrawn from the flow buffer (indicated by the arrow). The bound FL-BE dissociated and fluorescence decreased exponentially, (right) Reusability of the biosensor for multiple assays of cocaine introduced into the flow buffer after steady-state fluorescence (200 mV) was achieved. Cocaine at the indicated concentrations was added to the flow buffer for only the time intervals indicated by the bars. The downward deflection resulted from displacement of FL-BE by cocaine, but upon removal of cocaine from the flow buffer FL-BE displaced the bound cocaine. Reproduced with permission from reference 4, Copyright 1995 American Chemical Society.
The results obtained with carbonmonoxyhemoglobins with and without dithionite ion in the buffers indicate that the dithionite ion plays no significant role in the electrophoretic properties of the proteins. It is therefore of interest that ferrohemoglobin was found to have a lower isoelectric point in phosphate buffer than carbonmonoxyhemoglobin. Titration studies have indicated (5, 6) that oxyhemoglobin (similar in electrophoretic properties to the carbonmonoxy compound) has a lower isoelectric point than ferrohemoglobin in... [Pg.414]

Mix the labeled oligo sample with 12 1 of Ficoll load and load it in one of the gel pockets/slots. Run at 15 W. Check occasionally the bottom reservoir with the Mini-Minotor. Radioactivity in the buffer indicates that the excess [7- P]ATP has passed through the gel ( 2 hr). [Pg.342]

It is seen from the data that the area of the vesicle increases immediately after its exposure to the peptide buffer, indicating peptide insertion in the membrane. Also the insertion is pH dependent and increases when the pH is decreased from 7.5 to 5. With time, the increase of the apparent vesicle area reaches a semistationary value. For pH below 4.8, the membrane breaks down due to the action of the peptide. Data from experiments like this carried out over the whole pH range is summarized in Figure 9.20 which shows how the apparent vesicle area increases continuously with decreasing pH from 7.5 to 5.5 and then membranes become unstable below pH 4.8. [Pg.136]

Mixtures of a UV absorber, such as Tinuvin 326, and a HALS, such as Tinuvin 770, may be encountered. In this case the HALS, being a non-UV absorbing material, will not interfere with the determination of the UV absorber (as in section 2.2.2.2.3). However, although the UV absorber does not react with the buffered indicator reagent to form a yellow product, as does the HALS, it nevertheless absorbs in the region of 350-300 nm, distorting the... [Pg.14]

Mixture reacted with buffered indicator reagent and measured against chloroform. [Pg.14]


See other pages where Buffers indicators is mentioned: [Pg.95]    [Pg.684]    [Pg.502]    [Pg.253]    [Pg.217]    [Pg.58]    [Pg.518]    [Pg.127]    [Pg.441]    [Pg.141]    [Pg.122]    [Pg.123]    [Pg.877]    [Pg.58]    [Pg.589]    [Pg.285]    [Pg.126]    [Pg.664]    [Pg.122]    [Pg.150]    [Pg.128]    [Pg.32]    [Pg.263]    [Pg.13]   
See also in sourсe #XX -- [ Pg.780 , Pg.781 , Pg.782 ]




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