The action of carbonic anhydrase develops the carbonic acid, which on further disuniting releases the hydrogen ions and bicarbonate ions. The enzyme is detected in numerous organs including the brain, kidney, and eye, and the conversion of these gaseous molecules is processed by the carbonic anhydrase present in the red blood cells of the body. The enzyme has the capacity to undergo free dissociation after the formation and the ratio between the bicarbonate ions and the carbonic acid molecule ranges around 1:20. Thus the carbon dioxide is conveyed in the body in the form of bicarbonate ions. The bicarbonate ions undergo diffusion for the exchange of the chloride ions and the process is called the chloride shift. The ion exchange channel called the Band 3 mediated the exchange of the bicarbonate ions and the chloride ions in the cell. The red blood cell will attain a saturated state upon binding with maximum carbon dioxide molecule and thus permits no further addition of carbon dioxide molecules.
Transport of Carbon Dioxide with the Aid of Hemoglobin
The carbamino compounds are rapidly generated from the association of the uncharged amino groups. The association of the carbon dioxide molecule and the hemoglobin protein will result in the formation of carbaminohemoglobin. The presence of a large amount of the amino acid histidine in the hemoglobin makes it the only protein buffer of hydrogen ions. the amount of carbon dioxide discharged out of the body through the hemoglobin molecule ranges around 30%. The carbamino content of the blood is relatively low and the Haldane effect describes the difference in the carbon dioxide quantity between the deoxygenated and oxygenated hemoglobin molecules at the same partial pressure of carbon dioxide molecules. The deoxygenated hemoglobin molecule has a greater affinity to adjoin with the carbon dioxide molecules than the oxygenated hemoglobin. The conditions with lower partial pressure for the carbon dioxide molecule than the oxygen eases the association between the hemoglobin molecule and the carbon dioxide. The carbon monoxide gas possesses an even greater affinity to adjoin with the hemoglobin and it even has the capacity to displace the oxygen molecules.
Transport of Carbon Dioxide in Tissues
The combination of carbon dioxide and water forms carbonic acid and the reaction is found to be slower in the plasma and is accelerated in the red blood cells due to the presence of the enzyme carbonic anhydrase. The bicarbonate ions generated from the dissociation of the carbonic acid are found to diffuse from the erythrocytes into the plasma and the chloride ions are found to be conveyed into the red blood cells from the plasma. The imidazole moiety of the erythrocyte equips itself with a greater buffering capacity. The acidic state will favor the dissociation of the oxygen bond in the tissues and the buffering action of the hydrogen ions by the basic hemoglobin protein is observed. The basic nature of the histidine group in the hemoglobin favor the combination of the oxygen and hemoglobin and thus elevates the affinity of oxygen molecule with the loss of the carbon dioxide molecules. The affinity to bind with the oxygen molecule is elevated in the pulmonary capillary blood and the hemoglobin is found to discharge the carbon dioxide molecules. The oxygenated form of the hemoglobin tends to connect with fewer hydrogen ions and thus raises the acidic nature.
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