Title: Analysis of the effect of changing pressure on oxygen saturation and the effect of pH on haemoglobin-oxygen affinity using horse (Equus ferus) blood.
Introduction:
Haemoglobin is a protein molecule that is a component in red blood cells, the main purpose of haemoglobin is to carry oxygen from the lungs to tissues in the body as well as carrying carbon dioxide back to the lungs. The structure of haemoglobin gives it the ability to carry the oxygen our body need. Haemoglobin has a quaternary structure with 4 small subunits, 2 alpha and 2 beta (Bruno et al., 2008). These subunits each contain an Iron (Fe) atom, the ion containing compound is called the heme. This can bind one oxygen molecule each (Simoni et al., 1925), through ion-induced
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This helps one determine what the effects of increasing partial pressure effect how hemoglobin is able to hold onto oxygen. P50 is the point where the pressure of oxygen causes the saturation to be 50 %, haemoglobin with low affinity are have a higher P50 and haemoglobin with high affinity have a lower P50 (Collins et al., 2015).
In this experiment did 2 different trials one at 7.4 pH and one slightly acidic at 6.8 pH. The Bohr effect states that a reduction in pH reduces haemoglobin affinity and its carrying capacity which is also known as the root effect (Rummer and Brauner, 2015). Thus at lower pH haemoglobin would carry onto less oxygen and be a darker colour. The purpose of the lab was to determine the effect of the effect of changing PO2 on % oxygen saturation of Hb and examine the effect of pH on haemoglobin-oxygen affinity through the Bohr Effect. This was done through spectrophotometry measurements of horse haemolysate after being exposed to a vacuum at different pressures.
Due to theories above, it is speculated that oxygen saturation of haemolysate at lower pH, more acidic conditions, will have lower percentage transmittance overall as compared to the percentage transmittance of haemolysate kept under physiological pH at different partial
3ml of sample was taken first flask at 4 minutes and added to the appropriate tube of sodium hydroxide, from the second flask at 4.5 minute and so on, each flask was sampled at 30 second intervals. The sampling was then repeated starting at 8,12,16 minutes. The final sample from the last flask was taken at 18.5 minutes. Once the sampling was completed, measurements of absorbance were obtained for solution in each tube at 405 nm.
As the concentration of hemoglobin in the Red Blood Cells falls below normal, the total Red Blood Cell count consequently decreases. Therefore, oxygen cannot be adequately carried. (http://www.mayohealth.org/mayo/pted/htm/iron.htm).
To performed the experiment, a volumeter was set up to measure the net oxygen production under white light, then a second step was followed to measure oxygen consumption under dark conditions (oxygen production only happens in the presence of light and oxygen consumption in the presence of dark light) and finally, a third step consisted of recording the measure of the net oxygen production under the presence of green light.
As Pco2 rises, hemoglobin releases O2 more readily. Pco2 and pH are related factors because low blood pH (acidity) results from high Pco2.
K. How would you have expected Cari’s decreased Pco2 and alkaline blood pH to have affected her breathing?
“Erythrocytes contain haemoglobin, an important respiratory pigment that is essential for human life” (Strech, Beryl; Whitehouse, Mary;, 2010) Haemoglobin is very important because it is an iron-containing protein.
Figure 1: Amount of O2 gas curves to the time at which it was measured according to low, medium, and high pH.
The purpose of this virtual lab is to observe the acid-base balance in the urinary system by how PCO2 and blood pH affect the H+ and HCO3- in the urine. The renal compensation is a mechanism that shows the kidneys manage to change pH in correct way if the respiratory system is not healthy. The kidneys are two organs that help remove wastes and extra fluids out of the body. The acid-base balance is when the blood need to keep the balance of
Did the pH level of the blood change at all during normal breathing? If so, how? The pH did not change during the normal breathing.
Haemoglobin is a protein molecule found in red blood cells (RBC). Its role in the body is to transport oxygen from the lungs to the body 's tissues and then returns carbon dioxide from the tissues back to the lungs. The transportation of oxygen is only possible when haemoglobin (Hb) within the RBC binds to oxygen. (Martini & Nath, 2006)
The hemoglobin is determined using a non-cyanide analytical method from a dilution of whole blood.
HEMOGLOBIN Hemoglobin also spelled haemoglobin and abbreviated Hb or Hgb, is the iron-containing oxygen-transportmetalloprotein in the red blood cells of all vertebrates (with the exception of the fish family Channichthyidae) as well as the
Myoglobin maintains the same molecular structure regardless of the presence or absence of oxygen. While myoglobin is a single chain subunit that doesn’t display cooperate oxygen binding, hemoglobin is a four-subunit group with an abundant cooperativity to oxygen binding and greater oxygen affinity. Lactic acid produces hydrogen along with CO2 are actively found in metabolizing tissues in high concentrations. In the capillaries, the binding of allosteric effectors triggers the release of oxygen from hemoglobin in the capillaries, which the tissues reuptake in high affinity myoglobin before being delivered to the mitochondria. “The specific reaction of hydrogen ions and carbon dioxide with hemoglobin causing the release of O2 is called the Bohr effect” (Williams 2001).
* Percentage of hemoglobin (Hb) that is saturated with oxygen The oxygen saturation (SpO2) is a measure of how much oxygen the blood is carrying as a percentage of the maximum it could carry and is sometimes referred to colloquially as the "sats“ reading
Pulse oximetry is based around the principle that oxygenated Haemoglobin will absorb more light of certain specific wavelengths of light than deoxygenated haemoglobin and vice versa. Two wavelengths of light are used in pulse oximetry, red light of approximately 600nm, and infrared light with wavelengths of approximately 900nm. These two wavelengths of light are used to differentiate between two different substances, each with their own absorbance characteristics.