TY - JOUR
T1 - N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies
T2 - Acetylation of cytochrome c
AU - Nieman, Ronald A.
AU - Gust, Devens
AU - Cronin, John R.
N1 - Funding Information:
Support for this work was provided by the American Heart Association, Arizona Affiliate, and by the National Institutes of Health (GM 27200).
PY - 1982/3/1
Y1 - 1982/3/1
N2 - The reaction of N-[1-13C] acetylimidazole with cytochrome c and guanidinated cytochrome c was evaluated as a means of introducing NMR-detectable groups as conformation-dependent probes. Resonances from both N-[1-13C]acetyl lysyl and O-[1-13C]acetyl tyrosyl groups were observed when ferricytochrome c was acetylated. However, only O-[1-13C]acetyl tyrosyl resonances were seen with acetylated guanidinated ferricytochrome c. Chemical shifts of the four O-[1-13C]acetyl tyrosyl groups were conformation dependent and ranged from 172 to 176 ppm. A convenient method for the preparation of N-[1-13C]acetylimidazole is described.
AB - The reaction of N-[1-13C] acetylimidazole with cytochrome c and guanidinated cytochrome c was evaluated as a means of introducing NMR-detectable groups as conformation-dependent probes. Resonances from both N-[1-13C]acetyl lysyl and O-[1-13C]acetyl tyrosyl groups were observed when ferricytochrome c was acetylated. However, only O-[1-13C]acetyl tyrosyl resonances were seen with acetylated guanidinated ferricytochrome c. Chemical shifts of the four O-[1-13C]acetyl tyrosyl groups were conformation dependent and ranged from 172 to 176 ppm. A convenient method for the preparation of N-[1-13C]acetylimidazole is described.
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U2 - 10.1016/0003-2697(82)90356-6
DO - 10.1016/0003-2697(82)90356-6
M3 - Article
C2 - 6283939
AN - SCOPUS:0020110690
VL - 120
SP - 347
EP - 350
JO - Analytical Biochemistry
JF - Analytical Biochemistry
SN - 0003-2697
IS - 2
ER -