STUDIES ON THE HEMOGLOBIN-OXYGEN EQUILIBRIUM

The relation between the chemical structure a5d physiological function of hemoglobin was investigated with special reference to the role played by the protein moiety in the oxygen equilibrium function. The oxygenation of hemoglobin accompanies a reversible enormous hyperchromicity in the ultraviolet...

Full description

Saved in:
Bibliographic Details
Main Author: Tyuma,Itiro
Format: Report
Language:English
Subjects:
BIOCHEMISTRY
ELECTROPHORESIS
HEMOGLOBIN
LABORATORY ANIMALS
MOLECULAR STRUCTURE
PHYSIOLOGY
SOLUBILITY
ULTRAVIOLET SPECTROSCOPY
Online Access:Request full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The relation between the chemical structure a5d physiological function of hemoglobin was investigated with special reference to the role played by the protein moiety in the oxygen equilibrium function. The oxygenation of hemoglobin accompanies a reversible enormous hyperchromicity in the ultraviolet region and a marked increase in the resistance against alkali denaturation, suggesting a reversible conformation change in the protein moiety during the oxygenation. Heterogeneity of adult rat hemoglobin, which probably consists of six subcomponents, was substantiated by alkali denaturation and salting-out techniques. Fetalmaternal differences in molecular structure of hemoglobin were established in rabbits from the measurement of alkali denaturation rate, reactive SH content, and ultraviolet absorption spectrum, although both the hemoglobins exhibit the same homogeneous pattern on starch-gel electrophoresis. In oxygen equilibrium function, the fetal pigment shows a higher oxygen affinity and less Bohr effect than the maternal one, and these differences are ascribed to the differences in their molecular structure. (Author)