Accession Number : AD0666933

Title :   RELATION OF STRUCTURE TO FUNCTION IN HEMOGLOBIN.

Descriptive Note : Scientific Interim rept.,

Corporate Author : MINNESOTA UNIV MINNEAPOLIS DEPT OF CHEMISTRY

Personal Author(s) : Lumry,Rufus

Report Date : MAR 1968

Pagination or Media Count : 45

Abstract : The specific goals of this project were: (1) To establish the factors determining the oxygen affinity of mammalian hemoglobins. (2) To determine from these factors the basis for the serious inconsistencies now existing between quantitative observations on hemoglobin and the predictions from currently accepted models for hemoglobin. (3) To determine the factors influencing the oxygen-binding of mammalian myoglobin so as to establish reliable sets of experimental conditions for study of this protein. (4) To determine the degree of involvement of protein conformation in the oxygen-binding reactions of hemoglobin and myoglobin. (5) To provide a detailed quantitative description of the molecular mechanism of oxygen binding to hemoglobin and myoglobin. (6) To provide a basis for interpretation of the variation of the ligand-binding properties of blood under physiological conditions. (7) To establish the relationship between the effects of small anaesthetics such as xenon, cyclopropane and ethyl ether on the ligand-binding behavior of hemoglobin and myoglobin and their anaesthetic effects. Nitrogen gas also influences ligand-binding of myoglobin under certain circumstances. (8) To determine the quantitative relationships between the two major species of horse hemoglobin in their possible control of the aging of the horse erythrocyte. (Author)

Descriptors :   (*HEMOGLOBIN, BIOCHEMISTRY), MOLECULAR STRUCTURE, MOLECULAR ASSOCIATION, QUANTITATIVE ANALYSIS, ANESTHETICS, NITROGEN, ERYTHROCYTES, OXYGEN

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE