Microdetermination of ergocalciferol (vitamin D2) in pharmaceutical preparations by differential spectroscopy using trifluoroacetic acid in the absence of vitamin A.
A differential spectroscopy method for the determination of microgram quantities of ergocalciferol, using trifluoroacetic acid and hydrogen peroxide, was applied to commercially available pharmaceutical preparations. Tablets were powdered and extracted with methanol after being made basic with diethylamine. The methanol was concentrated, chloroform was added, and the mixture was chromatographed on neutral alumina using chloroform as the eluent. Ergocalciferol was determined in an aliquot of the eluate by differential spectroscopy and was compared with a reference ergocalciferol standard treated similarly. The method applied to low potency formulations (2.5-6 mug/tablet) is simple and quantitative, needs less than 5 hr for completion, and has a precision of less than +/- 2%. A simple and accurate chromatographic method for the determination of ergocalciferol in stabilized powders and high potency tablets, which precludes the necessity of solvent-solvent extraction, was also developed. The results are comparable with those obtained by the rat bioassay and the USP XVIII chemical assay.
Assay of vitamins in pharmaceutical preparations
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ProteinLens: a web-based application for the analysis of allosteric signalling on atomistic graphs of biomolecules
Abstract The investigation of allosteric effects in biomolecular structures is of great current interest in diverse areas, from fundamental biological enquiry to drug discovery. Here we present ProteinLens, a user-friendly and interactive web application for the investigation of allosteric signalling based on atomistic graph-theoretical methods. Starting from the PDB file of a biomolecule (or a biomolecular complex) ProteinLens obtains an atomistic, energy-weighted graph description of the structure of the biomolecule, and subsequently provides a systematic analysis of allosteric signalling and communication across the structure using two computationally efficient methods: Markov Transients and bond-to-bond propensities. ProteinLens scores and ranks every bond and residue according to the speed and magnitude of the propagation of fluctuations emanating from any site of choice (e.g. the active site). The results are presented through statistical quantile scores visualised with interactive plots and adjustable 3D structure viewers, which can also be downloaded. ProteinLens thus allows the investigation of signalling in biomolecular structures of interest to aid the detection of allosteric sites and pathways. ProteinLens is implemented in Python/SQL and freely available to use at: www.proteinlens.io.