Alder, George and Richards, John H. (1982) The Effect of DPG and IHP on the Relative Thermodynamic Affinity for CO of the Subunits of Rabbit Hemoglobin. In: Hemoglobin and Oxygen Binding. Elsevier , New York, NY, pp. 151-154. https://resolver.caltech.edu/CaltechAUTHORS:20150506-082657128
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Abstract
The two chains of most hemoglobins interact differently with ligands as can be seen in two nmr resonances for bound ^(13)CO (Moon and Richards, 1972). This observation has led to interest in the possibility that the two chains have different thermodynamic affinities toward ligands (Huestis and Raftery, 1973, 1975; Moon and Richards, 1974; Huang and Redfield, 1976; Viggiano and Ho, 1979a,b). Rabbit hemoglobin possesses an unusual α-chain which causes ^(13)CO bound to it to have a different chemical shift than ^(13)CO bound to β chains (Moon and Richards, 1972, 1974) and, thereby, allows direct quantitative observation of the degree of ligation of the two subunits.
| Item Type: | Book Section | ||||||
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| Additional Information: | © 1982 by Elsevier North Holland, Inc. This work was supported by the National Institutes of Health [Grants GM-16424 and HL-15162). | ||||||
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| Record Number: | CaltechAUTHORS:20150506-082657128 | ||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20150506-082657128 | ||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | ||||||
| ID Code: | 57254 | ||||||
| Collection: | CaltechAUTHORS | ||||||
| Deposited By: | Tony Diaz | ||||||
| Deposited On: | 06 May 2015 16:19 | ||||||
| Last Modified: | 03 Oct 2019 08:22 |
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