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This Concept Map, created with IHMC CmapTools, has information related to: Boron Chapter 29 - Transport of Oxygen and Carbon Dioxide in the Blood, Polycythemia Too many RBCs, leading to increase in blood viscosity and vascular resistance, As the 2,3-DPG concentration increases, hemoglobin shifts to a more tense state (Hb-O2 sat curve shifts towards the right) O2 affinity decreases, and more oxygen is released from the hemoglobin molecules*, Tensed vs. Relaxed state Relaxed state occurs when oxygen is bound to heme, causing the heme group to come down into the plane of the globin molecules, increasing O2 affinity, This effect leads to the sigmoidal hemoglobin saturation curve that we see as pO2 changes, Hemoglobin Structure of hemoglobin, Binds to hemoglobin with affinity that is 200X greater than oxygen. Decreases the available hemoglobin for O2 binding. Also causes hemoglobin's affinity for oxygen to increase dramatically --> hemoglobin does not release oxygen to the tissues as it should*, As the pCO2 increases, hemoglobin shifts to a more tense state (Hb-O2 sat curve shifts towards the right)* O2 affinity decreases, and more oxygen is released from the hemoglobin molecules*, Changes in the number of red blood cells (hematocrit) Polycythemia, Exists only as a monomer (ie only an α or β chain + a heme group) as a result Myoglobin only binds one molecule of O2 (compard to 4 by hemoglobin), Tensed state occurs when no oxygen is bound to heme, causing the heme group to be pushed slightly upwards, reducing O2 affinity Increases in pO2 cause hemoglobin to transition from a tensed state that cannot bind O2 to a relaxed state that does bind O2 This effect leads to the sigmoidal hemoglobin saturation curve that we see as pO2 changes, Globin chain surrounds the heme group Keep the O2 from binding irreversibly to the Fe2+ of the heme group, Myoglobin (hemoglobin's cousin that lives in the muscle) Exists only as a monomer (ie only an α or β chain + a heme group), Tensed state occurs when no oxygen is bound to heme, causing the heme group to be pushed slightly upwards, reducing O2 affinity, Heme group contains the iron atom Fe3+ cannot bind oxygen & is known as methemoglobin, Many additional factors shift the curve left or right depending on whether they cause the hemoglobin molecule to transition towards a tensed or relaxed state* pH, Found in red blood cells (RBCs) and is used to transport oxygen from the lungs to the tissues O2 content vs. saturation, Heme group plus a globin chain (α or β)* Globin chain surrounds the heme group, Found in red blood cells (RBCs) and is used to transport oxygen from the lungs to the tissues Changes in the number of red blood cells (hematocrit), Tensed vs. Relaxed state Tensed state occurs when no oxygen is bound to heme, causing the heme group to be pushed slightly upwards, reducing O2 affinity, Many additional factors shift the curve left or right depending on whether they cause the hemoglobin molecule to transition towards a tensed or relaxed state* 2,3-Diphosphoglycerate