Week 1

Domain knowledge

Enquiry and Research

 

In this week, I further reviewed the oxygen-hemoglobin dissociation curve

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figure.1

The oxygen dissociation curve is a graph that shows the percent saturation of haemoglobin at various partial pressures of oxygen. The purpose of an oxygen dissociation curve is to show the equilibrium of oxyhaemoglobin and nonbonded haemoglobin at various partial pressures.  At high partial pressures of oxygen, haemoglobin binds to oxygen to form oxyhaemoglobin.  When the blood is fully saturated all the red blood cells are in the form of oxyhaemoglobin.  As the red blood cells travel to tissues deprived of oxygen the partial pressure of oxygen will decrease.  Consequently, the oxyhaemoglobin releases the oxygen to form haemoglobin.

                                                                             
  Factors that influence oxygen binding, such as:

-Temperature
increasing the temperature denatures the bond between oxygen and haemoglobin, which increases the amount of oxygen and haemoglobin and decreases the concentration of oxyhemoglobin. The dissociation curve shifts to the right.

- 2,3-Diphosphoglycerate (DPG)

Is the main primary organic phosphate.  DPG binds to haemoglobin which rearranges the haemoglobin into the T-state, thus decreasing the affinity of oxygen for haemoglobin (T and R State).  The curve shifts to the right.

In the lecture it was a bit hard to understand the oxygen-hemoglobin dissociation curve however, after I did the reading I am able to understand the relationship between the factors that effects the curve. 

References

Marieb, E. N. (2012). Essentials of Human Anatomy & Physiology. (10^th ed.). San Francisco: Benjamin Cummings-Pearson Education.

Berne, R., Koeppen, B., & Stanton, B. (2010). Oxygen-hemoglobin dissociation curve .Retrieved April 8, 2016 from https://ankiweb.net/shared/info/1965989986