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fully saturated as OxyHb (four O  molecules) or   dissociation curve is due to the cooperation of
                                        2
             fully desaturated (DeOxyHb, no O ).         the  four oxygen  binding sites on the Hb mole-
                                         2
  VetBooks.ir  Hb-binding sites bound to oxygen. Due to the con-  cule. As the PaO  increases, SaO  rises rapidly as
               The term ‘SaO ’ refers to the percentage of total
                          2
                                                                                    2
                                                                       2
                                                         depicted by the steep slope of the curve. On the
             formational changes described above, Hb tends to
                                                         small changes in SaO  (e.g. 95% to 90%) actu-
             either be fully bound (oxygen on all four sites –   upper ‘flatter’ part of the curve, what seem to be
                                                                           2
             OxyHb – or deoxygenated). In other words, if 100   ally represents larger significant changes in oxy-
             Hb proteins had a SaO  of 75%, it would typically   gen concentration in the blood.  As the curve
                               2
             indicate 25 were fully desaturated as DeOxyHb   becomes steeper, relatively small losses of lung
             and 75 were fully saturated as OxyHb, as opposed   function affecting PaO  can result in relatively
                                                                            2
             to all 100 proteins each having three out of four   large changes in SaO .  The top of the curve is
                                                                           2
             binding sites filled with oxygen.           flattened because once all Hb molecules are fully
                                                         saturated (SaO  = 100%), no matter how much
                                                                      2
                                                         the PaO  is increased, no further gain in SaO  is
             Oxyhemoglobin dissociation curve                   2                             2
                                                         possible.
             How many Hb are fully saturated as OxyHb is   For  patients  who  are  breathing  room  air  and
             determined by the partial pressure of oxygen in the   therefore are still within the sigmoidal portion of
             plasma (PaO ). Oxygen diffuses from the alveolus   the  curve,  the  relationship  between  SpO   and
                       2
                                                                                            2
             into the plasma first and then loads onto Hb.   PaO  allows SpO  to be used as a surrogate marker
                                                                       2
                                                             2
             Conversely, when oxygen diffuses from the plasma   of PaO . For example, in a patient breathing room
                                                               2
             into the tissues, oxygen is released from the Hb   air with a pulse oximetry reading of 95%, it can be
             to replenish the plasma and allow for continued   assumed that the PaO  is approximately 70 mmHg.
                                                                          2
             oxygen diffusion into tissues.  The oxygen–hemo-  The relationship between the dissolved oxygen and
             globin  dissociation  curve  (Fig.  4.3)  describes  the   Hb-bound oxygen has significant clinical implica-
             relationship between the SaO  and the PaO .  tions for the total oxygen content able to be carried
                                    2
                                               2
               The dissolved oxygen (PaO ) is the independ-  in the blood as depicted in Box 4.1.
                                     2
             ent variable and is determined by lung function   The oxygen–hemoglobin dissociation curve is a
             (see Chapter 5). The sigmoid shape of the OxyHb   way to use the SpO  to approximate the PaO
                                                                                                2
                                                                          2
                                  100
                                   90
                                 Hemoglobin oxygen saturation (%)  60
                                   80
                                   70
                                   50
                                   40
                                   30
                                   20
                                   10
                                    0
                                     0           50           100          150
                                              Oxygen partial pressure (mmHg)
             Fig. 4.3.  The oxygen–hemoglobin dissociation curve describes the relationship between the percentage of Hb binding
             sites that are saturated with oxygen (SaO ) and the partial pressure of oxygen in arterial blood (PaO ) measured in
                                                                                    2
                                          2
             millimeters of mercury (mmHg). Open source illustration from https://www.researchgate.net/figure/Hemoglobin-Binding-
             Curve-Hemoglobin-oxygen-saturation-as-a-function-of-partial-pressure_fig10_309876232 (accessed 3 August 2019).

             Pulse Oximetry                                                                   73
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