Investigate the effect of altitude training on the density of blood.

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An Investigation to find out the Effect of Altitude Training on the Density Mock Blood

Rikin Patel

Candidate Number- 1110

Centre Number- 63255

Aim

The aim of this coursework was to investigate the effect of altitude training on the density of blood.

Introduction

Red blood cells, also known as Erythrocytes, are the most common type of  and are a 's principal means of delivering  to body tissues via the . The other type of blood cells in the blood are the white blood cells, which are actually .

Red blood cells deliver oxygen via , a complex molecule containing four  groups that temporarily link to oxygen molecules in the  and release the oxygen throughout the body. Hemoglobin also carries a  waste product,  back from the tissues. Red blood cells consist of almost 90% hemoglobin; the heme is what gives blood its . Myoglobin is similar to haemoglobin, but acts as a store for oxygen in  cells.

Human red blood cells have a flattened ovate shape, depressed in the center. This shape is used because it optimizes for the exchange of oxygen with the surrounding cells. The cells are flexible so as to fit through tiny , where they release their oxygen. The diameter of a typical red blood cell is . Below is a diagram of a red blood cell:

Red blood cells are continuously being produced in the red  of large bones. This production can be stimulated by a  called .

Red blood cells are broken down by a process called Hemolysis. Red blood cells normally live for 110 to 120 days and then die. When they die, they are broken down. The old cells swell up to a sphere and are engulfed by , they are destroyed and their materials are released into the blood. The hemoglobin is eventually excreted.

Haemoglobin is the substance that transports oxygen and is found in the red blood cells. It is an -containing -transport in the  of the  in humans. The molecule is mostly  mutations in the gene for the haemoglobin protein result in the hereditary diseases , as well as a group of diverse but rare diseases called .

At the centre of the molecule is a  ring, which is a ring like back bone whose atoms are not all of the same element. This ring is known as a  which holds an iron atom; this iron atom is the site of oxygen binding. An iron containing porphyrin is called a . The name hemoglobin is the derived from heme and globin, a  being a biological term for a .

In adult humans hemoglobin consits of two alpha and two beta subunits, which are not covalently bonded. The subunits are structurally similar and about the same size. Each subunit of hemoglobin contains a single , so that the overall binding capacity of adult human hemoglobin for oxygen is four oxygen molecules. Below is the structure of Haemaglobin:

The oxygen dissociation curve is a graph that shows the percent saturation of haemoglobin at various partial pressures of oxygen. There is a value that tells you the pressure at which the red blood cells are fifty percent saturated with oxygen. The purpose of an oxygen dissociation curve is to show the balance of oxyhaemoglobin and non-bonded haemoglobin at various partial pressures. At high partial pressures of oxygen, usually in the lungs, haemoglobin binds to oxygen forming oxyhaemoglobin. When the blood is fully saturated all the red blood cells are in the form of oxyhaemoglobin. As the red blood cells travel to tissues deprived of oxygen the partial pressure of oxygen will decrease. Therefore, the oxyhaemoglobin releases the oxygen to form haemoglobin

The sigmoid shape of the oxygen dissociation curve is a result of the mutual binding of oxygen to the four-polypeptide chains. Cooperative binding is the characteristic of haemoglobin to have a greater ability to bind oxygen after a subunit has bound oxygen. Thus, haemoglobin is most attracted to oxygen when three of the four-polypeptide chains are bound to oxygen.

Below is the oxygen dissociation curve, it shows the partial pressure of oxygen against the percent saturation of oxygen:

There are three factors that effect oxygen bonding, these three factors are:

  1. Temperature- increasing the temperature denatures the bond between oxygen and haemoglobin, which increases the amount of oxygen and haemoglobin and decreases the concentration of oxyhaemoglobin. Therefore dissociation curve shifts to the right.
  2. PH- a decrease in pH by addition of carbon dioxide or other acids causes the ‘Bohr Shift’. A Bohr shift is characterized by causing more oxygen to be given up as oxygen pressure increases and it is more pronounced in animals of smaller size due to the increase in sensitivity to acid. This causes the dissociation curve to shift to the right.
  3. Organic Phosphates- 2,3-Diphosphoglycerated (DPG) is the primary organic phosphate in mammals.  DPG binds to haemoglobin, which rearranges the haemoglobin, thus decreasing the affinity of oxygen for haemoglobin. The curve shifts to the right.
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Altitude effects on the Human Body- When a human body goes to a certain altitude then the body will attempt to maintain a state of homeostasis or balance to ensure the optimal operating environment for its chemical systems. Therefore the effect of increasing altitude on the human body will result in ability to provide adequate oxygen to carry out aerobic respiration. When a human body goes to altitude the main problem is the reduced ability to obtain oxygen form the atmosphere. This change may cause a rapid decline in the normally functioning of the body. If this is prolonged ...

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**** A detailed account of an investigation using mock blood. Good background information and clear presentation of statistical analysis. A level language used throughout. However, a slightly muddled grasp of concepts in places and a few factual errors.