How To Manage Blood Pressure Naturally

Hemoglobin and Oxygen transport

  1. Oxygen is transported by hemoglobin %98,5 and is dissolved in plasma %1.5
  2. At lower partial pressure, the hemoglobin resease oxygen.
  3. a shift of curve to the left because of an increase in pH, a decrease in carbon dioxide, or a decrease in temperature results in an increase in the ability of hemoglobin to hold oxygen.
  4. 0.3 ml O2 is found in 100 ml blood, otherwise 19.6 ml o2 is fund bound form in 100 ml blood.
  5. The binding of oxygen to the hemoglobin is determined by factors; po2 in alveolar air.
  6. Dissociation curve of oxygen is hyperboblic
  7. Increasing partial poressure in alveolar air increase the saturation of hemoglobin molecule with oxygen.
  8. As the po2 is 40 mmhg saturation still is 70%
  9. Oxygen-hemoglobin is almost completely saturated when PO2 is 80 mm Hg or above
  10. 1 gr hemoglobin can bind with 1.34 ml oxygen
  11. ıf the 1 ml blood include 15 gr hemoglobin, total bound oxygen easily calculated so that it is about 19.6 ml.
  12. The hemoglobin has a high percent saturation in arterial blood and lower percent saturation in venous blood.
  13. The effect of pH on the oxygen binding to the hemoglobin
  14. Lower pH increase dissociation of oxygen from hemoglobin
  15. Bohr effects shift the dissociation curve to left
  16. The effect of temperature on the dissociation of oxygen from hemoglobin. 

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Blood Type Genetics

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There are four types of respiratry pigment, hemoglobin, chlorocruorin, hemarythrin and hemocyanin.

There differ markedly in physical properties, structure, o2-binding site, O2 binding capacity, molecular weight and location.

Hemoglobin is bright red when oxygenated and ref blue when deoxygenated. Chlorocruorin is green. Hemerhythrin is violet pink when oxygenated and colorless when deoxygenated.

Hemocyanin is blue when oxygenated and colorless when deoxygenated.

Respiratory pigments are proteins that are specialized for the transport of O2. Myoglobin which resembles the subunit of hemoglobin is found fungi, plant/bacterial symbionts, protozoans and animals.

Annelida is the only phylum with representatives that have all types of respiratory pigment. Hemogloin and myoglobin are most common respiratory pigments in animals. Myoglobin is a from of hemoglobin located within muscle cells. circulating hemoglobin is commonly present in blood of nnelids with closed circulatory system.

it is dissolved in plasma for many species and located in homecytes for a few. Hemoglobin consist of variable numbe of subunit. Heme consist of a protoporphyrin molecule containing four pyrolle groups and ferrous ion at the center of the porphyrin.

The fe+2 can reversibly bind one O2 molecule. There are four polypeptide chain in globin part. Adult mammalian hemoglobin has two alfa and beta chains. Invertebrate hemoglobins which sometimes called erhythrocruorins may have many more than four heme subunits.

In some invertebrate and vertebrates animals two and multidomain hemoglobins.

composition of blood

Plasma and blood cells. Composition of plasma: electrolytes, organic molecules. Coelomic fluid differ in composition from that of circulatory fluids. Proteins in plasma and vertebrates and cephalopod mollusks have high plasma protein concentrations. Proteins is very important in osmotic pressure. Osmotic pressure due to proteins in called as colloid osmotic pressure.

  • immunglobulins
  • serum and plasma
  • the source of plasma components