Activity

Height is one of the most sensitive indicators of well-being because it combines the external influences of nutrition, economic wealth, health care, social equality, and other important socio-economic factors. The aim of this ecological study was to compare actual values of male and female height from 152 populations (except sub-Saharan Africa) with the mean supply of 47 food items from the FAOSTAT database (1995-2013) and mean values of seven socio-economic indicators (1995-2013). This comparison shows that economic wealth at the country level is only a mediocre correlate of physical growth because it is only loosely associated with the quality of nutrition and it does not reflect the social distribution of wealth. In a multiple regression model, the best predictors of stature are protein sources of the best and worst quality, and total fertility (which critically influences the amount of resources expended per child). In summary, these findings indicate that irrespective of crude economic statistics, the choice of specific nutrient sources and small family size are crucial factors determining the optimal physical development of children. Based on our data, we also believe that current international dietary recommendations regarding protein intake and protein quality would deserve serious re-evaluation. Different methods have been used for CYP3A phenotyping, such as probe drugs or the urinary index 6β-hydroxycortisol/cortisol ratio (6β-OHFC). This work describes a simple and affordable method for the simultaneous determination of the endogenous compounds cortisol and 6β-hydroxycortisol in urine using a background subtraction approach. The method was applied to investigate the CYP3A activity in HIV-infected pregnant women (n = 9) in the third trimester and postpartum periods. Also, the within-day variability in the 6β-OHFC index was also evaluated. The sample preparation consists of a pre-cleanup with acetonitrile followed by liquid-liquid extraction with ethyl acetate. The analytes were resolved by employing an Acquity UPLC®BEH C18 column with a mobile phase that consisted of a mixture of acetonitrile containing 0.1% formic acid and 0.1% formic acid in gradient mode. The method presented linearities of 1-1.000 ng/mL and 2-1.000 ng/mL for C and 6β-OHF, respectively, and presented acceptable precision and accuracy. Qualitative and quantitative matrix effects tests were also performed. A high 6β-OHFC within-day variability was observed in both phases. In the third trimester period, the 6β-OHFC ranged from 2.57 to 51.69, with a mean ± standard deviation (SD) of 15.12 ± 5.41 (n = 9). Similar values were obtained in the postpartum period, with 6β-OHFC ranging from 3.48 to 44.54 with a mean ± SD of 14.37 ± 5.73 (n = 7). Even though the 6β-OHFC is a non-invasive index for CYP3A phenotyping, its use is susceptible to high within-day variability. The quantitative determination of intact proteins in biological samples by LC with high-resolution MS detection can be a useful alternative to ligand-binding assays or LC-MS-based quantification of a surrogate peptide after protein digestion. The 22-kDa biopharmaceutical protein somatropin (recombinant human growth hormone) was quantified down to 10 ng/mL (0.45 nM) in 75 μL of rat plasma by the combination of an immunocapture step using an anti-somatropin antibody and LC-MS on a quadrupole-time of flight instrument. Accuracy and precision of the method as well as its selectivity and sensitivity did not depend on the width of the mass extraction window nor on whether only one or a summation of multiple charge states of the protein analyte were used as the detection response. Quantification based on deconvoluted mass spectra showed equally acceptable method performance but with a less favorable lower limit of quantification of 30 ng/mL. Concentrations in plasma after dosing of somatropin to rats correlated well for the deconvolution approach and the quantification based on the summation of the response of the four most intense charge states (14+ to 17+) of somatropin. Antimicrobial activity of cefoperazone, a high protein bound cephalosporin, depends on its unbound concentration. However, the protein binding data of cefoperazone in children is limited, making it challenging to optimize antimicrobial therapy in pediatric clinical practice. Furthermore, a validated method to measure the free part in children is unavailable with the small volume of samples that can be obtained. Therefore, in the present study, we developed and validated an LC-MS/MS method for the determination of free cefoperazone in children. In this study, 70 μL of plasma was used to prepare the ultrafiltrate (only containing the free drug). Chromatographic separation of the analyte was achieved on a C18 column using gradient elution with a mobile phase of acetonitrile and water (0.1% formic acid). Negative electrospray ionisation in the multiple reaction monitoring mode was applied for the detection of cefoperazone and ceftiofur (internal standard). AR-A014418 price The calibration curve was prepared in the range of 5-5000 ng/mL with excellent linearity. For each level of quality control samples, the intra- and inter-day precision (CV) was below 9.0%, and the accuracy ranged from 91.5% to 105.0%. The matrix effect was less than 11.7%, and the recovery was between 92.9% and 95.9% of cefoperazone. The validated method has been successfully applied to the determination of free plasma concentration of cefoperazone in pediatric patients. The results of the unbound fraction showed considerable individual variability (range 8.1-48.0%). The correlation analysis showed that age and albumin had significant effects on the protein binding of cefoperazone. Egg yolk phosvitin is of particular interest due to its functional and biological properties. Recently, it was demonstrated that high hydrostatic pressure (HHP) (400 MPa for 5 min) induced the transfer of folic acid and phosvitin from the egg yolk granule to the plasma fraction. A granule fraction (Gin) produced by egg yolk centrifugation was pressure-treated at 400 and 600 MPa for 5 and 10 min, and centrifuged to generate granule fractions (GP1 to GP4) and plasmas (PP1 to PP4). Iron and phosphorus contents were also increased in PP1 to PP4 fractions, confirming the transfer of phosvitins from pressure-treated granule to plasma. Pressurization drastically improved phosvitin recovery in PP fractions, specifically at 600 MPa for 10 min, which had the highest value of phosvitin/100 mg of dry plasma at 33.3 ± 4.39 mg. Consequently, HHP represents an alternative approach for phosvitin transfer and recovery in the egg yolk soluble fraction.