Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A,Boston, Iwate and Milwaukee |
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| Authors: | Gerd N La Mar Kiyoshi Nagai Thomas Jue David L Budd K Gersonde H Sick T Kagimoto A Hayashi F Taketa |
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| Institution: | 1. Department of Chemistry, University of California, Davis, CA 95616 USA;2. 2nd Department of Physiology, Nara Medical College, Kashihara 634, Japan;3. Department of Physiological Chemistry, TH Aachen, 5100 Aachen, Germany;4. 2nd Department of Internal Medicine, Kumamoto University Hospital, Kumamoto 860, Japan;5. 3rd Department of Internal Medicine, Osaka University Hospital, Osaka 530, Japan;6. Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226 USA. |
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| 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 mutated α chains. |
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