Spin-labeled hemoglobin.
- 1 July 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 56 (1) , 22-25
- https://doi.org/10.1073/pnas.56.1.22
Abstract
A preliminary study of the paramagnetic resonance spectrumof spin-labeled horse hemoglobin in solution is described. Evidence is strong that on oxygenation the B chains undergo a significant structural change near the reactive sulfhydryl gray (B 93) a change not yet resolved by X-ray diffraction. Features were found in the paramagnetic resonance spectra of nitroxide-maleimide spin-labeled hemoglobin that appear to be closely related to observations of Benesch Benesch on the inhibition of the Bohr effect by N-ethylmallimide.This publication has 11 references indexed in Scilit:
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