Blood oxygen affinity analyzer

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Found within the erythrocytes (red blood cells) of vertebrate blood, the respiratory pigment hemoglobin is a four-unit molecule consisting of two alpha- and two beta-globin polypeptide chains, each of which is bound to an iron-containing heme group (the site for oxygen-binding). Blood directly links external environmental conditions with cellular metabolic processes, hence the physiological properties of this molecule must be exquisitely tailored to balance the uptake of oxygen at the lung and its delivery to the tissues over a wide range of conditions. Because the heme groups of all vertebrate hemoglobins are identical, differences between the binding characteristics of vertebrate hemoglobins are reliant on the amino-acid composition of their globin chains, which can vary substantially between species. Indeed, changes of just a few amino-acid residues, resulting from base substitutions within the DNA of the alpha- and beta-globin genes, can have