Nuclear magnetic resonance studies of anaesthetic interactions with haemoglobin.
The use of 270 MHz Fourier Transform nuclear magnetic resonance (NMR) spectrometer, combined with signal processing techniques to improve resolution, enabled proton resonances from the individual aromatic residues of haemoglobin to be distinguished. In the presence of clinical concentrations of the general anaesthetic drugs halothane and methoxyflurane, specific changes in the NMR spectrum can be distinguished which probably reflect local changes of conformation. When higher concentrations of anaesthetic are used, extensive changes in the NMR spectrum occur which are consistent with non-specific binding of the anaesthetic to the hydrophobic parts of the haemoglobin molecule.
D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins; D006639:Histidine; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation; D008733:Methoxyflurane / Q000494:pharmacology*; D010649:Phenylalanine; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D014364:Tryptophan; D014443:Tyrosine
D006454:Hemoglobins; D011522:Protons; D008733:Methoxyflurane; D014443:Tyrosine; D010649:Phenylalanine; D006639:Histidine; D014364:Tryptophan