BIO 361 Lecture Notes - Lecture 14: Blood Gas Tension, Myoglobin, Deprotonation
10 Jul 2016
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Document Summary
One of the good ways to modulate oxygen binding to hemoglobin is to change the ph of the solution. This also gives us insight into how hemoglobin gets rid of carbon dioxide and protons in the body. There are different ways of describing the effect of ph on hemoglobin s oxygen binding properties. The bohr effect observed that hemoglobin appears to release protons (acts as a good acid) to the surrounding environment as oxygen is bound to hemoglobin. Conversely, as oxygen dissociates from hemoglobin, hemoglobin takes up protons. If hemoglobin enters an environment where there are many free protons (lower ph), this will help cause oxygen to come off proteins. Therefore, if hemoglobin enters an acidic tissue bed, it will release oxygen because the tissue bed is acidic which requires the oxygen due to its rapid metabolism. P50 is the pressure of oxygen required for half oxygen saturation. Higher p50, lower affinity for oxygen at lower ph (half of bohr-effect).
