Abstract
The proton nmr spectra of the synthetic valency hybrids, α2(β+CN)2, (α+CN)2β2 of hemoglobin A and the natural valency hybrids of the mutant hemoglobins Boston, Iwate and Milwaukee have led to the unambiguous assignment of the two proximal histidyl imidazole exchangeable proton signals at 64 and 76 ppm to individual α and β subunits, respectively. New single non-exchangeable proton resonances detected in the extreme downfield region of the spectra of Hbs Boston and Iwate are tentatively assigned to the coordinated tyrosine of the mutant α chains.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1172-1177 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 96 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1980 |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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la Mar, G. N., Nagai, K., Jue, T., Budd, D. L., Gersonde, K., Sick, H., Kagimoto, T., Hayashi, A., & Taketa, F. (1980). Assignment of proximal histidyl imidazole exchangeable proton nmr resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. Biochemical and Biophysical Research Communications, 96(3), 1172-1177. https://doi.org/10.1016/0006-291X(80)90075-3