Bone face reconstruction with polymethylmethacrylate.
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Bone Cements↗
Biomedical subjects
R Salas-Auvert
Publications and source records attributed to R Salas-Auvert.
Determination of anions in human and animal tear fluid and blood serum by ion chromatography.
An important factor contributing to the development of ion chromatography (IC) has been the need for repetitive analyses of samples with high ionic contents and samples available in microvolumes. IC was selected for the determination of Cl, NO3, SO(2-)4 and PO(3-)4 anions in tear fluid and serum from ten human volunteers of both sexes, seven young-adult black vultures (Coragyps atratus) and three young-adult chickens (Gallus gallus domesticus). The samples were analysed on a Dionex Model 2000i/SP ion-exchange chromatograph equipped with an anion guard column (Dionex IonPac AG4A), anion separator column (Dionex IonPac AS4A), suppressor column (Dionex AMMS-II) and a conductivity detector. The flow-rte of the mobile phase, 1.7 mM NaHCO3 - 1.8 mM Na2CO3 was set at 2.0 ml/min. The R.S.D. was calculated to be less than 1.5% for all anions. In the human, black vulture and chicken serum samples, the NO3, PO(3-)4 and SO(2-)4 anion contents were higher than in tears; for Cl the reverse was found. No correlation was found amongst the anion concentrations present in the tear fluid and blood serum in all samples (p > 0.05). With no sample treatment, column maintenance was required.
Adolescent↗
Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides.
Multiple linear regression was used to quantify the dependence of the antimicrobial activity of 13 peptides upon three calculated or experimentally determined parameters: mean hydrophobicity, mean hydrophobic moment, and alpha-helix content. Mean hydrophobic moment is a measure of the amphiphilicity of peptides in an alpha-helical conformation. Antimicrobial activity was quantified as the reciprocal of the measured minimal inhibitory concentration (MIC) against Escherichia coli. One of the peptides was magainin 2, and the remainder were novel peptides designed for this study. The multiple linear regression results revealed that the amphiphilicity of the peptides was the most important factor governing antimicrobial activity compared to mean hydrophobicity or alpha-helix content. A better regression of the data was obtained using ln(1/MIC+constant) as the dependent variable than with either 1/MIC or ln(1/MIC). These results should be useful in designing peptides with higher antimicrobial activity.
Amino Acid Sequence↗