PubMed · 4593154
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M Strauch, G Lux, R Ottenjann. 1973-11-16. [Reflux disease].. https://pubmed.ncbi.nlm.nih.gov/4593154/
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The pharmacokinetics of lignocaine was studied in four Icelandic horses after infiltration anaesthesia. A total of 240 mg of the drug was injected on either side of the left foreleg, over the medial and lateral branches of the palmar nerve. Blood samples were collected up to seven hours after injection and the concentrations of the drug in plasma were determined by gas chromatography/mass spectrometry. The results showed that lignocaine was rapidly absorbed. A mean maximum concentration of 232 ng/ml was observed after 20 minutes. In three of the horses the decline in the plasma concentration of the drug with time was best described by the sum of two exponential terms, but in one of the horses the decline was monoexponential. The mean half-life of the distribution phase (alpha) was 9.8 minutes and that of the elimination phase (beta) 48.4 minutes. In all the horses the plasma concentration was below the limit of detection (2 ng/ml) six hours after injection. Anaesthesia was tested in one horse and lasted for one hour.
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Tolperisone (1), a muscle relaxant with lidocaine-like activity, was compared to lidocaine (2) by molecular modeling methods. Conformational search analysis has been employed to find the global minima of these compounds along with numerous low energy conformations from which specific conformers were extracted that show good superimposition of the structural features important for protein binding. Two additional compounds, mepi- (3) and bupivacaine (4), were included in the analysis to validate the method as these ligands show very close structural and pharmacological relationship to lidocaine (2) and are assumed to bind to an identical site. As a result we find conformers of all four ligands that have exactly the same position and orientation of the potential sites for hydrogen bonding with the rest of the molecule showing close comparison of the three-dimensional geometry. Semiempirical calculations furthermore reveal good agreement of the electrostatic potentials of these conformations indicating similar interactions with a receptor. We conclude that tolperisone (1) and lidocaine (2) despite their chemical divergence can still attach to identical protein binding sites.