As it shifts to the right, it means that haemoglobin has a lesser affinity for oxygen
hemoglobin is the core of RBC'S and it has greater affinity to oxygen
The primary factor that determines how much oxygen is actually bound to hemoglobin is the partial pressure of oxygen (pO2) in the hemoglobin solution.
The oxygen-haemoglobin dissociation curve, also spelled oxygen-hemoglobin dissociation curve, plots the proportion of hemoglobin in its saturated form on the vertical axis against the prevailing oxygen tension on the horizontal axis. The oxyhemoglobin dissociation curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO2) and partial pressure of oxygen in the blood (PO2), and is determined by what is called "hemoglobin's affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it. found on wikipedia
Ph and temperature
The affinity of hemoglobin for CO is roughly 20,000 times greater than that of oxygen in vitro. In vivo, the affinity of hemoglobin for CO is roughly 200-225 greater than that of oxygen. ------------------------------------------------------------------------------------------------- O2 has stronger bond than CO. Therefore, the oxygen in CO loves the iron in the hemoglobin as iron ends with two electrons which complete the 6 electrons in the oxygen. In vivo, the affinity of hemglobin for CO is about 153 from 141x153/141. by amin elsersawi
The rise of temperature denatures the bond between oxygen and hemoglobin.
Yes. This an example of the Bohr effect. If pH is lower than normal (normal is 7.4), then hemoglobin does not bind oxygen as well. The higher the pH, the lower the H ion concentration, the lower the carbon dioxide level, and the GREATER affinity hemoglobin has for oxygen. The binding of oxygen to hemoglobin in the lungs is not affected by changing the pH.
It increases the bloods affinity to oxygen and buffers carbonic acid in the blood.
BPG in hemoglobin means allosteric effector, that binds to the site that is completely remote from that active site for oxygen. The amount of BPG in red cells determines the oxygen affinity of hemoglobin.
number of red blood cells
Hemoglobin is a protein that is carried by red blood cells. Homoglobin needs oxygen to be carried by the cells. Without it, the body does not receive enough protein.
When CO is not ventilated it binds to hemoglobin, which is the principal oxygen-carrying compound in blood; this produces a compound known as carboxyhemoglobin. The traditional belief is that carbon monoxide toxicity arises from the formation of carboxyhemoglobin, which decreases the oxygen-carrying capacity of the blood and inhibits the transport, delivery, and utilization of oxygen by the body. The affinity between hemoglobin and carbon monoxide is approximately 230 times stronger than the affinity between hemoglobin and oxygen so hemoglobin binds to carbon monoxide in preference to oxygen. ~ Wikipedia.