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02.16.11 - 100ml of whole blood is 15ml of hemoglobin and...

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100ml of whole blood is 15ml of hemoglobin and then dissolve that into 100 ml plasma, the hemoglobin is what dissolves how much oxy. Can dissolve into the blood. So what happens at the alveoli surface is that every aspect of mass. Transp. Equ. Is being modified…the sa of lungs is quite large…walls of alveoli are very thin and flattened..a single layer…the blood cells are stacked in there one by one bc the cap. Are so thin….max. transp. Coeff. And minimal vol….conc. gradient is max. in two ways…because hb can hold 100 times more oxy….and forms a sink…the oxy. Blood is being moved away from the site of exchange. And replaced by deoxygenated blood…fig. 1s. Hb is a protein coded by two diff. genes…has four subunits…two are subcoded by alphaglobin gene and two by betaglobin gene…when prot. Have m ultiple. Subunits there are a number of things that could potent. Happen…allosteric modification is a change in the shape of the protein…caused by a change in the shape of the other molecules in the protein fig. 2.….binding oxygen is something that changes the shape…and binding site. Consequences of are…fig. 3 when stuff is oxygen and stuff disss. Is hb it looks like second line…sigmoidal shape curve…fig. 4 oxygen dissociation curve…the conc. Of oxy. In arterial blood is about 100…when deoxy hb is moving towards a siteof high oxy levels…it quickly gains affinity for them and gains them on….if it offloads all this oxy. Cause the local oxy. Load back up…in those actively metabolizing tissues there is another protein called myoglobin…has a higher affinity for otwo than oxyg. Esp. in low oxy. Environment…..good question….it is in tissue..it pours down the sink into oxymyoglobin. It also moves from a region of high ph to low ph which has a consequence. Because it goes towards carbonic acid…if right shift curve…in low oxy. And low ph..has even lower affinity for binding oxy…come off more easily…Bohr shift…fig. 5….if we wereto plot the course….
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