PubMed · 14911820
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R A PETERS. 1952-02-28. Lethal synthesis.. https://doi.org/10.1098/rspb.1952.0001
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The electron impact mass spectrometric properties of trimethylsilyl ether and fluoroacyl ester derivatives of trenbolone, combined or not combined with a methoxime group, are presented. Some derivatization problems were observed and were due to the formation of enol derivatives at the 3C-position in several tautomeric forms, which in their turn were not stable and lost two or four hydrogens under the conditions studied. The enolization could be minimized by carefully selecting the reaction conditions or could be prevented by the introduction of a methoxime group at the 3C-position. The limits of detection and identification of the methoxime heptafluorobutyryl ester and the methoxime trimethylsilyl ether derivative of trenbolone were determined using a mass selective detector in the electron impact mode and a triple-stage quadrupole in the methane positive chemical ionization mode. Selected reaction monitoring in tandem mass spectrometry did not improve the limit of detection, but because of the gain in selectivity did improve the limit of identification. The glucuronides of trenbolone and epitrenbolone could be identified in three urine specimens out of 200 samples in routine doping control.
The toxicity of guar gum, derived from the Indian leguminous plant Cyamopsis tetragonolobus, is thought to be due to a globulin which can be denaturated and made non-toxic. Another very toxic compound, fluoroacetic acid, has been detected at a low level in raw samples of guar gum (0.07-1.42 micrograms fluoroacetic acid/g). A sample of a guar-gum pharmaceutical formulation contained only 0.08 ppm fluoroacetate. One exceptionally high value of 9.5 micrograms/g was found in a guar-gum powder. The low concentrations of fluoroacetate found in guar gum dispel any considerations about possible health risks associated with fluoroacetate during the prolonged use of guar gum at the recommended doses.
High-field (270 MHz) 1H-NMR has been employed to study the solution conformation of glycophorin A, a sialoglycoprotein which spans the human erythrocyte membrane. Glycophorin A is one of the most fully characterized integral membrane proteins known, making it an excellent model for the study of membrane-bound proteins. This protein consists of three distinct domains: a glycosylated extracellular N-terminus, a hydrophobic intramembranous segment, and a polar cytoplasmic C-terminus. These domains contain aromatic residues which serve as convenient 1H-NMR conformational probes. The aromatic region of the NMR spectrum of glycophorin A in 2H2O shows single, well-resolved His and Tyr resonances. No resonances are observed, however, for the Phe residues which are located in or near the hydrophobic domain. These observations suggest that considerable heterogeneity with respect to segmental motions exists within the protein. This is consistent with circular dichroism data showing the intramembranous segment to be completely helical with the extremities of the protein being predominantly random coils. The helix of the hydrophrobic domain is remarkably resistant to conventional denaturing conditions including variations in pH, and temperature, and treatment with guanidine hydrochloride. However, in trifluoroacetic acid, which strongly solvates peptide backbones, there is extensive reversible unfolding of the helical structure as evidenced by the appearance of Phe resonances. Solvent titration experiments indicate that approximately a 1 : 1 volume ratio of trifluoroacetic acid to 2H2O is required to initiate unfolding of the helix.