Assignment of proximal histidyl imidazole exchangeable proton nmr resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee

G. N. la Mar, K. Nagai, Thomas Jue, D. L. Budd, K. Gersonde, H. Sick, T. Kagimoto, A. Hayashi, F. Taketa

Research output: Contribution to journalArticle

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Abstract

The proton nmr spectra of the synthetic valency hybrids, α2+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 languageEnglish (US)
Pages (from-to)1172-1177
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume96
Issue number3
DOIs
StatePublished - 1980

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ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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