Stock solutions (50 mM in DMSO-d6) of the appropriate compounds were prepared. After dilution of 11 μl with 100 μl Millipore water and 189 μl DMSO-d6 to 1.9 mM hydrolysis solutions the reaction was started by the addition of 300 μl PBS (50 mM, pH 7.3). The solution was incubated at 37 °C in a thermomixer. An initial aliquot (25 μl) was taken directly and analysed by analytical HPLC at 265–266 nm. Further aliquots were taken for monitoring the kinetic hydrolysis. The exponential decay curves (pseudo-first order) based on absolute integral values were calculated with commercially available software (OriginPro 9.0G) and yielded the half-lives t1/2(1) and t1/2(2) of the prodrugs via one determination.
Originpro 9.0g
Manufactured by OriginLab
Sourced in United States
OriginPro 9.0G is a data analysis and graphing software. It provides tools for data import, manipulation, analysis, and visualization.
Automatically generated - may contain errors
Lab products found in correlation
5 protocols using originpro 9.0g
1
Kinetic Hydrolysis Analysis of Prodrugs
2
Statistical Analysis of Experimental Data
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Statistical analyses were performed using
the OriginPro 9.0G software. p values were computed
using an unpaired or paired Student’s t test,
where appropriate. For the statistical analysis of multiple groups,
one-way analysis of variance was used followed by Tukey’s test.
A p value of 0.05 was considered significant. All
data are presented as means ± the standard error of the mean
unless otherwise stated.
the OriginPro 9.0G software. p values were computed
using an unpaired or paired Student’s t test,
where appropriate. For the statistical analysis of multiple groups,
one-way analysis of variance was used followed by Tukey’s test.
A p value of 0.05 was considered significant. All
data are presented as means ± the standard error of the mean
unless otherwise stated.
3
Statistical Analyses in OriginPro 9.0G
4
Voltage-Gated Channel Activation Kinetics
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Boltzmann relationships were fitted with OriginPro 9.0G by where Vh is the voltage of half-maximum activation and zδ the effective gating charge. F, R, and T are the Faraday constant, the molar gas constant, and the temperature in Kelvin, respectively. I is the actual current amplitude and Imax the maximum current amplitude at the saturating hyperpolarizing voltage of −150 mV specified for each patch. All current amplitudes in the absence of cAMP were additionally normalized to Imax at saturating cAMP.
The time courses of current activation and deactivation were fitted with a single exponential starting after an initial delay: where A is the amplitude, t the time, and τ the time constant for either activation or deactivation.
Experimental data are given as mean ± SEM.
The time courses of current activation and deactivation were fitted with a single exponential starting after an initial delay: where A is the amplitude, t the time, and τ the time constant for either activation or deactivation.
Experimental data are given as mean ± SEM.
5
Analyzing Concentration-Activation and Binding
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Concentration-activation relationships were analyzed by fitting the Hill equation (eq 7) to the individual current data using the OriginPro 9.0G software (Northampton, USA): 1 (7) , with I being the actual current amplitude, Imax the maximal current amplitude at a saturating ligand concentration, EC50 the concentration of half-maximum activation, and HA the Hill coefficient of activation. Experimental data are given as mean ± SEM. Concentration-binding relationships were analyzed by fitting the Hill equation (eq 8) to the mean fluorescence data using the OriginPro 9.0G software (Northampton, USA): 1 (8), with F being the actual fluorescent intensity, Fmax the maximal fluorescent intensity at a saturating ligand concentration and saturating voltage, BC50 the concentration of halfmaximum binding, and HB the Hill coefficient of binding.
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