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A comparative study on the structural differences of primate hemoglobins by spin labeling technique.

S Nakayama·M Aoki·T Watanabe·O Takenaka·K Takahashi·M Hoshino·M Yoshida
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Abstract

The hemoglobins of human and five non-human primates were spin-labeled with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide, and the ESR spectra of their deoxy, oxy, and carbonmonoxy forms were measured. The analyses of the spectra indicated that the local protein conformation in the vicinity of the spin-labeled cysteine residue at position 93(F9) in the beta-chain is slightly but significantly different among species, and that each hemoglobin shows a similar change in conformation upon conversion from the oxy form to the carbonmonoxy one except for human hemoglobin. Human hemoglobin was suggested to undergo a significantly different conformational change upon this conversion, indicating that it has unique characteristics among the primate hemoglobins.

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AnimalsCarboxyhemoglobinElectron Spin Resonance SpectroscopyHemoglobinsHumansOxyhemoglobinsPrimatesProtein ConformationComparative StudyJournal Article

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S Nakayama, M Aoki, T Watanabe, O Takenaka, K Takahashi, M Hoshino, M Yoshida. 1988. A comparative study on the structural differences of primate hemoglobins by spin labeling technique.. https://doi.org/10.1093/oxfordjournals.jbchem.a122519

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