13 C NMR Spectra of Allosteric Effectors of Hemoglobin
Abstract
In the last three years many papers dealing with the preparation and biological activity of compounds that act as allosteric effectors of hemoglobin have been published. Among the numerous moieties, some urea derivatives were found to be very effective in reducing oxygen affinity of hemoglobin. The structures of most of the compounds were confirmed by 1H NMR spectra; however, to our knowledge, 13C NMR spectra have not been published for any of these allosteric modifiers of hemoglobin. We prepared in this series over 30 new urea and thiourea derivatives with the intent of investigating their biological activity. An analysis of 13C NMR spectra revealed high regularity in the chemical shifts of the similar fragments of the structures and revealed signal deviations among structures having different substituents in the aromatic rings.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1993
- Accession Number
- ADA262979
Entities
People
- Stanislaw Ostrowski
- Thomas G. Burke
- Waldemar Priebe
Organizations
- Ohio State University