Carbon-13 NMR studies of 13CO binding to human hemoglobin |
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Authors: | P J Vergamini N A Matwiyoff R C Wohl T Bradley |
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Institution: | Los Alamos Scientific Laboratory, University of California, Los Alamos, NM 87544 USA;Hematology Section Veterans'' Administration Hospital San Francisco, CA 94121 USA |
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Abstract: | In the 13C NMR spectrum of hemoglobin A carbonylated with 13CO, separate resonances can be distinguished at 207.04 ppm and 206.60 ppm (with respect to the 13C resonance of external tetramethyl-silane) for 13Co bound to the α and β chains of the hemoglobin tetramer. A study of the 13Co derivatives of the isolated α and β chains, and of the abnormal hemoglobin MIWATE which contains α chains which are in the met Fe(III)] form and do not bind CO, has permitted an assignment of the high field (206.60 ppm) resonance to the β chain 13CO and the low field one to the α chain 13CO. The identification of these 13Co resonances permits a study of the differences in the chemistry of the α and β heme units in intact hemoglobin. Some results on the differences in the redox behavior of these chains are included. |
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