Transfer processes in animal coats. II. Conduction and convection

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Abstract
The perturbation of haemoglobin by halothane has been studied as a model system for the interaction of a general inhalational anaesthetic agent with a protein. These interactions have been studied with Fourier transform n.m.r. techniques, and differences between the haemoglobin proton spectra in the absence and presence of halothane have been recorded over a range of pH values and anaesthetic concentrations. These have revealed a small number of conspicuous perturbations which were found to persist down to clinical concentrations of halothane, and over the whole pH range studied. These perturbations, which were also observed in haemoglobin in whole red cells, strongly suggest either that the invasion of the protein surface and interior by the anaesthetic is a very selective process, or that the protein only allows very specific distortions to occur. Assignments have been offered for the histidine C2 resonances involved in the perturbation, and are based on comparisons between human and various animal oxyhaemoglobins, and studies with human oxy- and deoxyhaemoglobin. By using these assignments, an attempt has been made to locate the area of strongest interaction between halothane and haemoglobin through the perturbations which manifest themselves at the molecular surface at or near the titrateable histidine residues.

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