RELATION OF STRUCTURE TO FUNCTION IN HEMOGLOBIN.
Abstract
A summary of two years of research is given. Nearly all previous work on oxygen-binding of myoglobin has been shown to be in error because of contaminants. A purification procedure has been developed and the thermodynamic changes in oxygen binding to contaminated and pure myoglobin have been determined. The fundamental errors in the current lore on the mechanism of oxygenation of hemoglobin have been analyzed in detail leading to the hypothesis that oxygen binding is not measured by spectral changes which are primarily due to a change in spin state. New and more powerful methods for handling oxygen-binding data have been developed. Methods of higher precision for the determination of oxygen and carbon-monoxide in hemoglobin solutions have been developed or are nearly the required level of precision. A fundamental and ubiquitous property of liquid water important in small-solute as well as protein reactions appears to have been identified. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 31, 1968
- Accession Number
- AD0701094
Entities
People
- Rufus Lumry
Organizations
- University of Minnesota