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Blood consists of two different types of hemoglobin: oxyhemoglobin is bound to oxygen, while deoxyhemoglobin is unbound to oxygen. These two different types of hemoglobin exhibit different absorption spectra that are normally represented in terms of molar extinction coefficients, as shown in Figure 1.
A CO-oximeter measures the absorption of light passing through blood from few as two or three wavelengths of light to several dozens of wavelengths, in order to distinguish oxyhemoglobin, and deoxyhemoglobin (formerly called 'reduced' hemoglobin), and thus determine the oxyhemoglobin saturation (the percentage of oxygenated hemoglobin compared to the total amount of available hemoglobin (Hb)).
In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). [5] Hemoglobin has an oxygen-binding capacity of 1.34 mL of O 2 per gram, [ 6 ] which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. [ 7 ]
Through a process called the haemodynamic response, blood releases oxygen to active neurons at a greater rate than to inactive neurons. This causes a change of the relative levels of oxyhemoglobin and deoxyhemoglobin (oxygenated or deoxygenated blood) that can be detected on the basis of their differential magnetic susceptibility.
Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO 2) and partial pressure of oxygen in the blood (PO 2), and is determined by what is called "hemoglobin affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it. Structure of oxyhemoglobin
The onset of neural activity leads to a systematic series of physiological changes in the local network of blood vessels that include changes in the cerebral blood volume per unit of brain tissue (CBV), changes in the rate of cerebral blood flow, and changes in the concentration of oxyhemoglobin and deoxyhemoglobin.
The average red blood cell contains 250 million hemoglobin molecules. [7] Hemoglobin contains a globin protein unit with four prosthetic heme groups (hence the name heme-o-globin); each heme is capable of reversibly binding with one gaseous molecule (oxygen, carbon monoxide, cyanide, etc.), [8] therefore a typical red blood cell may carry up to one billion gas molecules.
Since the globin fold contains only helices, it is classified as an all-alpha protein fold. The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the first protein fold discovered (myoglobin was the first protein whose structure was solved).