Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas
Abstract:
The isolated beta subunit of hemoglobin Kansas has an oxygen affinity that is as low relative to the oxygen affinity of the beta(A) subunit as the affinity of hemoglobin Kansas is low relative to hemoglobin A. Thus the low affinity properties of hemoglobin Kansas are almost completely reflected in the properties of the isolated subunits. The kinetic results show that the equilibrium affinity difference results both from a much larger oxygen dissocation rate constant in beta(Kansas) (k = 37 sec(-1) and 18 sec(-1) for beta(Kansas) and beta(A), respectively) and from a lower association reaction rate, The properties of the alpha chains from hemoglobins A and Kansas appear to be identical, as expected.
More Related Videos
08:31Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
09:24Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
Published on: May 8, 2026
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Cooperative Allosteric Transitions
Respiration and Gaseous Exchange
Respiration involves the exchange of gases, especially oxygen (O2) and carbon dioxide (CO2), between the alveoli and body cells, a process facilitated by blood circulation. As a result, the cardiovascular system, which involves the...
Hemoglobin
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Oxygen Transport in the Blood
