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STUDIES OF HEME-PROTEINS.
Final rept. 21 Aug 64-31 Oct 66,
MINNESOTA UNIV MINNEAPOLIS LAB FOR BIOPHYSICAL CHEMISTRY
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Techniques were developed for preparing homogeneous hemoglobin free of contaminants and detailed studies were conducted on association and dissociation of the hemoglobin tetramer as a function of salt concentration. Binding of oxygen and carbon monoxide ligands to hemoglobin as indirectly observed by spectrophotometric techniques lack agreement with predictions based on the Adair mechanism. A theoretical basis for this discrepancy was developed in this laboratory and preliminary experimental data utilizing direct gasometric measurements show that a method is now available to directly measure heme-heme interaction and that much of the present literature on the subject may be incorrectly interpreted. The binding of xenon to myoglobin was examined in detail. At least two xenon binding sites interact cooperatively with the binding of carbon monoxide and a small molecule contaminant links this ligand-ligand interaction. Thermodynamic studies on myoglobin implicate important conformational changes during ligand binding. Author
APPROVED FOR PUBLIC RELEASE