Gas Carriage Notes
This is a sample of our (approximately) 3 page long Gas Carriage notes, which we sell as part of the Respiratory System Notes collection, a 60-70% package written at Bristol University in 2012 that contains (approximately) 49 pages of notes across 17 different documents.
The original file is a 'Word (Docx)' whilst this sample is a 'PDF' representation of said file. This means that the formatting here may have errors. The original document you'll receive on purchase should have more polished formatting.
Gas Carriage Revision
The following is a plain text extract of the PDF sample above, taken from our Respiratory System Notes. This text version has had its formatting removed so pay attention to its contents alone rather than its presentation. The version you download will have its original formatting intact and so will be much prettier to look at.
Lecture 7 Gas carriage
Explain the difference between PaO2, SaO2 and CaO2 o PaO2
Partial pressure of oxygen dissolved in blood (mmHg ) o SaO2
Percentage saturation of haemoglobin with oxygen
Sigmoidal relationship to PaO2 o CaO2
Total volume of oxygen contained per unit volume of blood (ml)
Depends on volume bound to Hb and volume dissolved in blood Using the oxyhaemoglobin dissociation curve, explain the relationship between PaO2
& CaO2 o SaO2 = (amount of oxygen bound to Hb/oxygen binding capacity) X 100
Describe the effect of a voluntary breath hold upon arterial saturation o Causes a fall in arterial saturation with O2 o If held for long enough can fall below 90 o Experiment in lecture Describe the use of pulse oximeter o Indirectly monitors the oxygen saturation of a patient's blood o Acceptable normal ranges for patients (without COPD etc.) problem are 95 to 99%
o How it works
Pair of small LEDs facing a photodiode through a translucent part of the patient's body, usually a fingertip or an earlobe.
One LED is red and the other is infrared
Absorption at these wavelengths differs significantly between oxyhemoglobin and its deoxygenated form Describe and explain the carriage of O2 by haemoglobin o Primary function of hemoglobin (Hb) is to transport oxygen o O2 not very soluble in water, so oxygen transport protein must be used to allow oxygen to be 'soluble' o Iron is the site of oxygen binding; each can bind one O2 molecule thus each hemoglobin molecule is capable of binding a total to four (4) O2 molecules o Primary factor that determines how much oxygen is actually bound to hemoglobin is the partial pressure of oxygen (pO2) in the hemoglobin solution
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