Seal hemoglobin has a higher affinity for oxygen than human hemoglobin, allowing seals to efficiently extract oxygen from their environment during prolonged dives. Additionally, seal hemoglobin can undergo changes in its structure at low oxygen levels to further enhance oxygen binding. These adaptations help seals thrive in their aquatic environment.
Yes, a low pH (acidic environment) decreases hemoglobin's affinity for oxygen. This is known as the Bohr effect, where pH and carbon dioxide levels affect oxygen-hemoglobin binding. In an acidic environment, hemoglobin releases oxygen more readily to tissues where it is needed.
It decreases the amount of Red blood cells that can transport O2 because smoking decrease the hemoglobin activity.
Haldane effect
No it does not.
Bohr effect. Incorrect. It is not the Bohr effect...it is actually the "Haldane effect"=The lower the PO2 and the lower the extent of hemoglobin saturation with oxygen (O2), the more CO2 can be carried in the blood. This phenomenon is called the Haldane effect. As per the Human Anatomy and Physiology eighth edition text book published 2010.
increasing the concentration increases the rate of the reaction
increasing the concentration increases the rate of the reaction
increasing the concentration increases the rate of the reaction
By lowering the blood plasma level, the red blood cells are concentrated.
An increase in pCO2 (partial pressure of carbon dioxide) can lead to a decrease in oxygen transport because it can shift the oxygen-hemoglobin dissociation curve to the right, reducing the affinity of hemoglobin for oxygen. This means that hemoglobin will release oxygen more readily, making it less efficient in transporting oxygen to tissues.
It doesn't.