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

doi:10.1016/0006-291X(80)90075-3

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

Biochemistry and Molecular Medicine

Research output: Contribution to journal › Article

58 Scopus citations

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	https://doi.org/10.1016/0006-291X(80)90075-3
State	Published - 1980

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ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

Cite this

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

Assignment of proximal histidyl imidazole exchangeable proton nmr resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. / la Mar, G. N.; Nagai, K.; Jue, Thomas; Budd, D. L.; Gersonde, K.; Sick, H.; Kagimoto, T.; Hayashi, A.; Taketa, F.

In: Biochemical and Biophysical Research Communications, Vol. 96, No. 3, 1980, p. 1172-1177.

Research output: Contribution to journal › Article

la Mar, GN, Nagai, K, Jue, T, Budd, DL, 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, vol. 96, no. 3, pp. 1172-1177. https://doi.org/10.1016/0006-291X(80)90075-3

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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 mutant α chains.",

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AU - la Mar, G. N.

AU - Nagai, K.

AU - Jue, Thomas

AU - Budd, D. L.

AU - Gersonde, K.

AU - Sick, H.

AU - Kagimoto, T.

AU - Hayashi, A.

AU - Taketa, F.

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N2 - 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.

AB - 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.

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10.1016/0006-291X(80)90075-3