A novel flow partition device for spirometry during large animal anaesthesia.

OBJECTIVE: We describe and test a novel device for large animal anaesthesia monitoring that uses standard human medicine spirometry sensors. STUDY DESIGN: In-vitro study. METHODS: The device consists of two adapters that enable the flow to be split evenly into four tubes in parallel, each tube containing a D-lite sensor. The performance of this flow partitioning device (FPD) over a range of flows from 100 to 700 L minute⁻¹ was determined and the pressure versus flow relation, resistance and dead space was compared with a Horse-lite (Moens 2010). RESULTS: Equipped with four D-lite sensors, and a flow of 700 L minute⁻¹ the pressure drop of the FPD was 13.5 cm H2O, resistance 1.17 cm H2O second L⁻¹ and volume (potential dead space) 182 mL, compared to 2.8 cm H2O, 0.24 cm H2O second L⁻¹ and 54 mL respectively for the Horse-lite. The predicted value of the flow partition of » could be confirmed. Limits of agreement were found to be 4.2% in inspiratory direction and 7.1% in expiratory direction. CONCLUSIONS AND CLINICAL RELEVANCE: The FPD is an affordable device that extends the specification of any commercially available human spirometry sensors to large animal applications. However, an increase in total resistance and dead space has to be taken into account. Therefore, the new device could be useful during equine anaesthesia.

Exploring the cross-reactivity of S25-2: complex with a 5,6-dehydro-Kdo disaccharide.

The near-germline antibody S25-2 exhibits a remarkable cross-reactivity for oligosaccharides containing the bacterial lipopolysaccharide carbohydrate 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo). The recent synthesis of a variety of Kdo analogues permits a detailed structural analysis of the importance of specific interactions in antigen recognition by S25-2. The Kdo disaccharide analogue Kdo-(2→4)-5,6-dehydro-Kdo lacks a 5-OH group on the second Kdo residue and has been cocrystallized with S25-2. The structure reveals that the modification of the Kdo residue at position 5 results in a rearrangement of intramolecular hydrogen bonds in the antigen that allows it to assume a novel conformation in the antibody-combining site. The cross-reactive binding of S25-2 to this synthetic ligand highlights the adaptability of this antibody to non-natural synthetic analogues.

Screening for illicit drugs on Euro banknotes by LC-MS/MS.

A method for the simultaneous quantification of illicit drugs on Euro banknotes, using an ultra-performance liquid chromatography tandem mass spectrometry, was developed and validated. The method included cocaine, benzoylecgonine, MDMA, MDEA, MDA, methamphetamine, diacetylmorphine, 6-MAM, morphine and Δ(9)-THC. Drug residues were monitored and quantified via positive ESI mode using multiple reaction monitoring. Banknotes were extracted with methanol by vigorous shaking. Recovery rates were in the range of 60-80%. Calibration was performed with spiked banknotes in the range of 10-100 ng/note (R(2) 0.98-0.99). Intra-day analysis showed fair precision and accuracy (≤ 15%). Matrix effects were in the range from 27% to 235%. 7-15 samples of each denomination were analyzed. The calculated median values per note were 106 ng cocaine, 43 ng benzoylecgonine, 41 ng heroin, 15.5 ng 6-MAM, 16.5 ng morphine, 9 ng MDMA and 7 ng methamphetamine. Δ(9)-THC was detected on 4 banknotes. MDEA and MDA were not detected on any note. A widespread background contamination for cocaine and opiates was demonstrated.

Synthesis and antigenic properties of C-7-modified Kdo mono- and disaccharide ligands and Kdo disaccharide interresidue lactones.

In order to define binding interactions of Kdo-specific monoclonal antibodies directed against the chlamydial alpha-(2-->8)-linked Kdo disaccharide epitope on a molecular level, modifications at the 7-position of the proximal and distal Kdo unit were investigated. The synthesis of 7-O-methyl and 7-azido-7-deoxy-7-epi-Kdo monosaccharide derivatives was achieved via an 8-O-TBS protected derivative, whereas methylation of O-7 at the proximal Kdo unit of the alpha-(2-->8)-linked Kdo disaccharide was conveniently accomplished via a 4,5; 4',5'; 7',8'-tri-O-carbonyl-protected disaccharide intermediate. Attempted epimerization at C-5 of the inner unit of a alpha-(2-->4)-linked Kdo disaccharide, however, resulted in formation of the corresponding 5,6-dehydro derivative, which was fully deprotected. Treatment of unprotected alpha-(2-->8)- as well as alpha-(2-->4)-linked Kdo disaccharides in neat acetic acid furnished the corresponding interresidue lactone derivatives. The lactones displayed limited stability under neutral conditions and were hydrolyzed at pH 7 within 3 days. Access to the lactones, however, provides a means for selective derivatization of the carboxylic group located at the distal Kdo residue, which was demonstrated by methanolysis of the lactone to afford the monomethyl ester of the alpha-(2-->8)-linked Kdo disaccharide. ELISA inhibition experiments of the ligands with two Kdo-specific monoclonal antibodies showed slightly reduced reactivity for the binding of the alpha-(2-->8) Kdo-specific antibody S25-2, whereas the 7-O-methyl disaccharide antigen displayed high binding affinity toward the Kdo monosaccharide-specific antibody S67-27.