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Examination of the aspirin acetylation site of human serum albumin by ^13^C NMR spectroscopy by J. T. Gerig; K. E. Katz; J. D. Reinheimer; Glenn R. Sullivan; John D. Roberts is a Chemistry article available to read on EtoBox.

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## Abstract Human serum albumin has been specifically acetylated using aspirin in which the methyl carbon of the acetyl group was enriched to 90% ^13^C. A single resonance at 23.13 ppm downfield from tetramethylsilane was observed in ^13^C differences spectra obtained at both 25.2 and 45.3 MHz. Chemical shift studies of several model compounds suggest that this is the resonance position to be expected for an acetamide group exposed to solvent. The line width observed for the enriched methyl resonance is consistent with free rotation of the methyl group.

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Author

J. T. Gerig; K. E. Katz; J. D. Reinheimer; Glenn R. Sullivan; John D. Roberts

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; John Wiley and Sons Ltd; Wiley (ISSN 0749-1581)

Published

1981

Language

EN

Field

Chemistry (Physical Sciences)