Hemoglobin Function
Globin Portion
Consisits of amino acids linked together to form a polypeptide chain. Synthesized in the Ribosomes.
OD shift to the left
Hemoglobin has a higher attraction and affinity for oxygen. Decrease in 2,3-DPG, reduced body temperatures, and alkalosis.
Heme Portion
Involves four iron atoms in the ferrous state (Fe2+). Surronded by the protoporphyrin ring (structure formed in the nucleated red blood cells). Synthesized in the mitochondria.
Hemoglobin
Life giving substance of every blood cell, the oxygen carrying component of the red blood cell. A protein, the main cytoplasmic component of the erythrocyte. Picks up oxygen from the lungs and releases it in the tissues.
OD shift to the right
More likely to release oxygen to the tissues. Lower affinity, anemia, acidosis, Increased CO2 levels, and higher body temperature.
2,3-Diphosphoglycerate (2,3-DPG)
Produced via the Embden-meyerhof pathway during anaerobic glycolysis. Intimatly related to oxygen affinity of hemoglobin.
Oxygen Dissasociaton Curve
Represents oxygen release from hemoglobin to the tissues.
Allosteric Changes
The way hemoglobin is able to rotate on its axis, determine the action of salt bridges between the globin structures, and dictate the movement of 2,3-DPG. Has two forms tense and relaxed.
