Lab 2 Flashcards
What are the major functions of hemoglobin?
Hemoglobin is a protein found in red blood cells that plays a crucial role in transporting oxygen from the lungs to the rest of the body. The major functions of hemoglobin include:
Oxygen transport: Hemoglobin binds to oxygen in the lungs and carries it to the body’s tissues and organs. The oxygen is released from hemoglobin when it reaches the tissues that need it.
Carbon dioxide transport: Hemoglobin also helps transport carbon dioxide, a waste product of cellular metabolism, from the body’s tissues back to the lungs where it can be exhaled.
Acid-base balance: Hemoglobin helps regulate the pH of the blood by binding to and releasing hydrogen ions. This helps maintain the proper balance of acids and bases in the blood.
Nitric oxide transport: Hemoglobin can also bind to and transport nitric oxide, a signaling molecule that helps regulate blood pressure and blood flow.
Define: anemia; polycythemia.
Anemia is a condition in which there is a lower than normal number of red blood cells or a lower than normal amount of hemoglobin in the blood. Hemoglobin is the protein in red blood cells that carries oxygen to the body’s tissues. Anemia can result in a variety of symptoms, including fatigue, weakness, shortness of breath, pale skin, and dizziness. It can be caused by a variety of factors, including iron deficiency, vitamin deficiency, blood loss, or chronic diseases.
Polycythemia is a condition in which there is an abnormally high number of red blood cells in the blood. This can lead to thickening of the blood and an increased risk of blood clots. Symptoms of polycythemia may include headaches, dizziness, fatigue, and blurred vision. Polycythemia can be caused by a variety of factors, including genetic mutations, chronic hypoxia (low oxygen levels), or certain medical treatments.
Describe the structure of hemoglobin. What is a possible cause of anemia?
Hemoglobin is a complex protein that is made up of four subunits, each of which contains a heme group. The heme group is a complex molecule that contains iron, which is responsible for binding to oxygen.
Each subunit of hemoglobin is made up of two parts: a globin protein and a heme group. The globin protein is made up of a sequence of amino acids that fold into a specific shape. There are two types of globin protein chains in hemoglobin: alpha and beta.
Anemia can be caused by a variety of factors, including:
Iron deficiency: Iron is necessary for the production of hemoglobin, so a lack of iron can lead to anemia.
Vitamin deficiency: Vitamins such as vitamin B12 and folate are also necessary for the production of red blood cells, so a deficiency in these vitamins can lead to anemia.
Blood loss: A significant loss of blood, such as from an injury or surgery, can lead to anemia.
Genetic disorders: Certain genetic disorders can affect the production or function of hemoglobin, leading to anemia.
Chronic diseases: Chronic diseases such as kidney disease, cancer, and autoimmune disorders can interfere with the production of red blood cells, leading to anemia.
Do you think it is advantageous for a football player to breathe in 100% O2 while resting on the sidelines between plays? Why or why not?
No, it is not advantageous for a football player to breathe in 100% oxygen while resting on the sidelines between plays.
Although oxygen is necessary for cellular respiration and energy production in the body, breathing 100% oxygen does not significantly increase the amount of oxygen that the body can use. The amount of oxygen that the body can use is limited by the body’s ability to transport it to the tissues, not by the amount of oxygen available in the air.
Furthermore, breathing 100% oxygen can actually be harmful to the body in certain circumstances. It can increase the risk of oxygen toxicity, which can cause lung damage, seizures, and other health problems.
Carefully draw the oxygen dissociation curve. What happens to it during moderate exercise in which muscle temperature increases, lactic acid is produced, and the volume of CO2 produced per min (VCO2) is increased?
During moderate exercise, several factors can cause the oxygen dissociation curve to shift to the right. These factors include an increase in muscle temperature, an increase in lactic acid production, and an increase in the volume of CO2 produced per minute (VCO2). These changes in the body result in a decrease in blood pH, which causes the hemoglobin to release oxygen more readily.
The shift to the right in the oxygen dissociation curve means that at any given partial pressure of oxygen (PO2), hemoglobin will release more oxygen to the tissues. This allows the muscles to receive the oxygen they need to perform work during exercise, even when the partial pressure of oxygen in the blood is lower.
What are the significance of the plateau and the steep portion of the O2-Hb dissociation curve?
The significance of the plateau on the oxygen-hemoglobin dissociation curve is that it represents the range of partial pressures of oxygen in which hemoglobin is almost completely saturated with oxygen. This means that small changes in PO2 within this range have little effect on the amount of oxygen that is bound to hemoglobin. The plateau is important because it ensures that even when the partial pressure of oxygen in the blood is lower, there is still a high percentage of hemoglobin that is carrying oxygen, which is necessary to maintain adequate oxygen delivery to the tissues.
The steep portion of the oxygen-hemoglobin dissociation curve represents the range of partial pressures of oxygen in which hemoglobin is only partially saturated with oxygen. This means that small changes in PO2 within this range can have a significant effect on the amount of oxygen that is bound to hemoglobin. The steep portion is important because it allows for efficient unloading of oxygen in the tissues that require it the most. For example, during exercise or at high altitudes where the partial pressure of oxygen is lower, the steep portion of the curve ensures that hemoglobin releases oxygen to the tissues that need it the most.
Explain the dangers of carbon monoxide poisoning as it relates to hemoglobin function.
When inhaled, carbon monoxide enters the bloodstream and binds to hemoglobin with a much higher affinity than oxygen, forming carboxyhemoglobin (COHb). This binding of CO to hemoglobin reduces the amount of hemoglobin available to carry oxygen, leading to a decrease in oxygen delivery to the tissues.
Given the following values, calculate the total O2 content of the blood in ml O2/100 ml.
Hb concentration = 15.9 g/100 ml PaO2 = 90 mmHg
SpO2 = 92%
To calculate the total oxygen content of blood, we need to use the formula:
Total Oxygen Content (ml O2/100 ml) = (Hb x 1.34 x SaO2) + (0.003 x PaO2)
Where:
Hb = Hemoglobin concentration in g/100 ml
1.34 = Oxygen-binding capacity of hemoglobin (ml O2/g)
SaO2 = Arterial oxygen saturation expressed as a decimal
0.003 = Dissolved oxygen in blood (ml O2/mmHg/100 ml)
PaO2 = Partial pressure of arterial oxygen in mmHg
Given:
Hb concentration = 15.9 g/100 ml
PaO2 = 90 mmHg
SpO2 = 92% (converted to SaO2 = 0.92)
Total Oxygen Content = (15.9 g/100 ml x 1.34 ml O2/g x 0.92) + (0.003 x 90 mmHg)
Total Oxygen Content = 20.2 ml O2/100 ml
Therefore, the total oxygen content of blood in this case is 20.2 ml O2/100 ml.
