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Published August 1974 | public
Journal Article

^(13)C magnetic resonance studies of the binding of carbon monoxide to various hemoglobins

Abstract

Carbon monoxide binding to hemoglobins from a variety of sources has been studied by ^(13)C nuclear magnetic resonance. The two resonances have been specifically assigned to ^(13)CO bound to α or to β subunits. The reason for the anomalous shift of ^(13)CO bound to the a chain of rabbit hemoglobin is discussed with particular reference to residue Phe-48 (CD6). The relative facility with which oxygen displaces carbon monoxide, and the relative thermodynamic affinity for carbon monoxide compared to the unliganded state, of the α and β subunits are found to differ.

Additional Information

© 1974 American Chemical Society. Received October 16, 1973. Supported by U.S. Public Health Service Grants NIHL 15198 and NIHL 15162. We thank M. Nelson for assistance with the chain separations and F. Brown for electrophoresis studies. We also wish to thank Dr. D. Powars of the Los Angeles County-USC Medical Center for providing samples of sickle cell and fetal blood.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023