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The CDDP plasma protein binding rate in both CDDP alone group and CDDP co-administration with ZMYL group for the individual sampling time point were determined (Fig. 6).
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However, antibiotics with high protein binding require special consideration since, classically, it is accepted that only the unbound fraction of the compound is active in vitro and presumably in vivo; the different protein binding rate in mice and humans limiting the extrapolation of results for high protein binding antibiotics.
The binding rate, in particular, may be influenced by the exact nature of the DNA substrate, whether plasmid or junction, or completely dsDNA.
Thus an oxygen-insensitive process is not a major cause of the high binding rate in oesophageal mucosa, and may not contribute significantly to the observed binding in other normal tissues.
Apart from exploring combined effects of antibiotics and the immune system, the study arms consisting in antibiotic administration alone (in non-immunized animals) provided interesting pharmacodynamic information on cefditoren and ceftriaxone, considering their similar protein binding rates in mice and humans.
The crucial issue was how the average binding rate fluctuates on a larger timescale, i.e., do the large variations in binding rates in each time-step average-out at a larger timescale and if so, how small can this timescale be?
Additionally, Dox has a more prolonged half-life and a greater plasma protein binding rate [ 2], both in humans and animals.
However, other measures of potency, such as area under the curve (AUC), were not considered to see whether increasing the binding rate resulted in increased potency in general.
However, kinetic analysis of the results of a PET study of [11C]doxepin showed 30% specific binding in the monkey brain, and a larger specific binding rate (36%) in the human brain [33].
We will show how the computations change while we consider a certain concentration of siRNA molecules for deriving the overall binding rate subsequently in this section.
Manipulation of the (distal) heme cavity architecture is often reflected by changes in both binding rates as well as in the strength of binding of cyanide to the ferric heme iron.
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