Oxygen Transport

Descripción

(Respiratory) Physiology 1B Mapa Mental sobre Oxygen Transport, creado por Daniel Elandix G el 06/09/2013.
Daniel Elandix G
Mapa Mental por Daniel Elandix G, actualizado hace más de 1 año
Daniel Elandix G
Creado por Daniel Elandix G hace más de 11 años
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Resumen del Recurso

Oxygen Transport
  1. Composition of Alveolar Air At Rest

    Nota:

    • Average: Oxygen: 100mmhg Carbon dioxide: 40mmHg Water Vapour: 47mmHg Nitrogen: 573mmHg
    1. Venous And Arterial Blood Gas Tension

      Nota:

      • Blood composition changes as it passes thru the lungs, gas exchange at the alveoli. Blood coming from Pulmonary Artery: Oxygen: 40mmHg Carbon Dioxide: 47mmHg Blood coming from lungs into pulmonary vein: Oxygen: 100mmHg Carbon Dioxide: 40 mmHg Arterial blood:Blood from pulmonary arteries with bronchial veins and left ventricle.Oxygen: 95mmHgCarbon Dioxide: 40 mmHg
      1. Blood Oxygen Transport

        Nota:

        • Dissolved and carried in blood in 2 forms: Dissolved Combined with haemoglobin
        1. Haemoglobin

          Nota:

          • Molecular weight of 64450KDs, 4 subunits which also consists of a haem molecule connected in a polypeptide chain. 2 alpha chains (141aa) and 2 beta chains (146 aa) The haem molecule consists of a porphyrin derivatiive and one atom of Ferrous Fe2+.
          1. Quarternary Structure

            Nota:

            • Quarterany structure aids in loading of the oxygen molecules. Available in 2 states Tense and Relaxed. It is also allosteric. I.e when one molecule binds, it enables the other molecules to bind to them easier.
        2. Oxygen capacity, saturation and content

          Nota:

          • 3 terms to remember: Oxygen Capacity: Amt of o2 which can combined with Hb. at normal its 15g/100ml. Oxygen Saturation: Percentage of available binding sites for Hb to attach. Saturation Formula: O2 with Hb/O capacity X 100 Oxygen Content: Amt of molecular oxygen that is released after destroying binding power of Hb.
          1. Equation to determine O2 content

            Nota:

            • (1.34 X Hb X Sat/100)+ 0.003 X Partial Pressure Oxygen Saturation is 97.5% for normal Hb 1.34 is constant for Hb 0.003 is the solution constant for Oxygen
          2. Hb-O2 equilibrium curve

            Nota:

            • Important factors that shift the curve to the right. increase in H conc i.e pH decreases Increases in temperature Increases in carbon dioxide conc increase in 2,3 diphosphoglycerate (2,3 DPG) notable points Partial pressure of oxygen vs % Saturation 0 vs 0 20 vs 35 27 vs 50 40 vs 75 100 vs 97.5 Flat upper portion shows the o2 loading of the lungs The steep lower portion shows the o2 diffusion into the tissues.
            1. Bohr Effect

              Nota:

              • Shift the OEC due to the change in blood pH and Co2. hydrogen ions bind to the histidine residues on Hb and hence initiates conformational changes and it decreases affinity towards oxygen This leads to enhanced oxygenation of blood in the lungs and release of oxygen in tissues.
              1. 2,3 DPC

                Nota:

                • Produced by glycolysis of RBC binds to deoxyHB therefore decrease affinity of oxygen binding.
              2. Haemoglobin vs Myoglobin

                Nota:

                • Different type, oxygen storage in muscle.  Binds to one oxygen
                1. CO poisoning

                  Nota:

                  • CO has higher affinity to Hb. Forms carboxylhaemoglobin. Symptoms of patient will be hypoxic. But no cyanosis. COHb will be cherry red in color.
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