Samuel L. MacKenzie, D. Tenaschuk, G. Fortier
1987
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0
Influential Citations
59
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Journal
Journal of chromatography
Abstract
The effect of temperature, solvent and reagents on the formation of the N(O)-dimethyl-tert.-butylsilyl derivatives of proteic amino acids has been studied. Quantitative silylation is achieved using dimethyl-tert.-butylsilyltrifluoroacetamide with 1% tert.-butyldimethylchlorosilane in dimethylformamide by heating at 75 degrees C for 30 min. Two peaks were obtained for arginine under these conditions. However, most of the standard proteic amino acids can be assayed. The N(O)-dimethyl-tert.-butylsilyl derivatives of the proteic amino acids have been analysed by gas chromatography-mass spectrometry using the methane chemical ionization mode. The spectral data are presented and have been used to confirm the structures of the amino acid derivatives.