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NMR study of the sites of human hemoglobin acetylated by aspirin

โœ Scribed by Arron S.L Xu; Jeffrey M Macdonald; Richard J Labotka; Robert E London

Book ID
114149961
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
507 KB
Volume
1432
Category
Article
ISSN
0167-4838

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Examination of the aspirin acetylation s
Examination of the aspirin acetylation site of human serum albumin by 13C NMR spectroscopy
โœ J. T. Gerig; K. E. Katz; J. D. Reinheimer; Glenn R. Sullivan; John D. Roberts ๐Ÿ“‚ Article ๐Ÿ“… 1981 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 386 KB

## 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. Che