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.