Abstract
The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl group of the Val-E11 resonates in a clear spectral region at -2.76 ppm and responds to dynamic changes in cellular oxygenation. With CO, the signal shifts to -2.4 ppm. The Val-E11 peak assignment and its response to oxygen and CO agree perfectly with previous myoglobin solution studies. Intracellular oxygen level can now be determined in vivo with the signal intensity ratio of oxymyoglobin/deoxymyoglobin, reflected by the Val-E11 and His-F8 peaks in the 1H NMR spectra. Moreover, protein structure-function relationship in vivo can now be probed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4731-4733 |
| Number of pages | 3 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 89 |
| Issue number | 10 |
| State | Published - 1992 |
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ASJC Scopus subject areas
- Genetics
- General
Cite this
Observing the1H NMR signal of the myoglobin Val-E11 in myocardium : An index of cellular oxygenation. / Kreutzer, Ulrike; Wang, Donc S.; Jue, Thomas.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 10, 1992, p. 4731-4733.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Observing the1H NMR signal of the myoglobin Val-E11 in myocardium
T2 - An index of cellular oxygenation
AU - Kreutzer, Ulrike
AU - Wang, Donc S.
AU - Jue, Thomas
PY - 1992
Y1 - 1992
N2 - The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl group of the Val-E11 resonates in a clear spectral region at -2.76 ppm and responds to dynamic changes in cellular oxygenation. With CO, the signal shifts to -2.4 ppm. The Val-E11 peak assignment and its response to oxygen and CO agree perfectly with previous myoglobin solution studies. Intracellular oxygen level can now be determined in vivo with the signal intensity ratio of oxymyoglobin/deoxymyoglobin, reflected by the Val-E11 and His-F8 peaks in the 1H NMR spectra. Moreover, protein structure-function relationship in vivo can now be probed.
AB - The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl group of the Val-E11 resonates in a clear spectral region at -2.76 ppm and responds to dynamic changes in cellular oxygenation. With CO, the signal shifts to -2.4 ppm. The Val-E11 peak assignment and its response to oxygen and CO agree perfectly with previous myoglobin solution studies. Intracellular oxygen level can now be determined in vivo with the signal intensity ratio of oxymyoglobin/deoxymyoglobin, reflected by the Val-E11 and His-F8 peaks in the 1H NMR spectra. Moreover, protein structure-function relationship in vivo can now be probed.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026610882&partnerID=8YFLogxK
M3 - Article
VL - 89
SP - 4731
EP - 4733
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 10
ER -