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Why should the increased affinity of crocodile hemoglobin for bicarbonate ion allow the crocodile to hold its breath for long periods of time?
Like most systems in the body (any body) the oxygen delivery system doesn't work at 100% efficiency - it's just good enough to keep us going. The blood returning to the heart and lungs hasn't given up all the oxygen it carries, just some of it. In crocodiles, as more bicarbonate ions attach to the hemoglobin cell, it loosens the hold on the remaining oxygen, allowing it to be released to be used by the body. So the crocodile hemoglobin/oxygen system is more efficient than a human's, and that lets them go longer without breathing, if they have to.
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Which interactions and processes contribute to the dissolution of ionic compounds in water?
The process of providing energy to break ionic bonds and allow soluble ionic compounds to dissolve in water?
What is a antonym of hydrophobia?
An antonym of hydrophobia is hydrophilic, which means having an affinity for water rather than a fear of it.
How can the oxygen store in myoglobin be replaced after use?
Myoglobin has a very high affinity for oxygen, meaning it binds it very strongly. At very low oxygen concentrations in the cell, myoglobin releases its oxygen, despite the high affinity, simply because there are too few oxygen molecules around to rebind to the myoglobin when they are released naturally from the myoglobin (which usually occurs anyway). Once the oxygen concentration increases again, returning to normal, oxygen molecules will collide with myoglobin. The myoglobin, with its high oxygen affinity, will strongly bind any oxygen that meets it, replenishing myoglobin's oxygen storage very quickly. As myoglobin's affinity for oxygen is stronger the haemoglobin's, it will 'steal' oxygen from haemoglobin in the blood very easily, replacing its bound oxygen. This binding system serves to release oxygen when it is needed if blood oxygen levels are reduced (due to high levels of exercise), but replenishes the supply when oxygen levels begin to rise again.
Who had a horse called Magnolia?
The horse Magnolia belonged to Ulysses S. Grant, who was the 18th President of the United States. Grant had a strong affinity for horses and enjoyed riding and caring for them.
What are the adaptations of a yak?
Indigenous mountain animals like the llama, alpaca, and vicuña in the Andes or the yak in the Himalayas are adapted rather than acclimatized to the low oxygen partial pressures of high altitude. Their hemoglobin has a high oxygen affinity, so that full saturation of the blood with oxygen occurs at a lower partial pressure of oxygen. In contrast to acclimatized humans, these indigenous,...
What are the factors that affect hemoglobin's affinity for oxygen?
The primary factor that determines how much oxygen is actually bound to hemoglobin is the partial pressure of oxygen (pO2) in the hemoglobin solution.
How many time greater is the affinity of hemoglobin for carbon monoxide greater than the affinity of hemoglobin for oxygen?
The affinity of hemoglobin for CO is roughly 20,000 times greater than that of oxygen in vitro. In vivo, the affinity of hemoglobin for CO is roughly 200-225 greater than that of oxygen. ------------------------------------------------------------------------------------------------- O2 has stronger bond than CO. Therefore, the oxygen in CO loves the iron in the hemoglobin as iron ends with two electrons which complete the 6 electrons in the oxygen. In vivo, the affinity of hemglobin for CO is about 153 from 141x153/141. by amin elsersawi
In anemia 23-DPG is and oxygen affinity is?
In anemia, 2,3-DPG (2,3-diphosphoglycerate) levels are typically elevated. This compound decreases the affinity of hemoglobin for oxygen, helping to release oxygen to the tissues. Consequently, oxygen delivery to tissues may be improved despite the lower hemoglobin levels in anemia.
What does NOT affect hemoglobin's affinity for oxygen?
Hemoglobin's affinity for oxygen is not directly affected by factors such as the presence of carbon dioxide in the bloodstream or the pH level of the blood. While these factors can influence the oxygen-binding capacity through the Bohr effect, they do not change the intrinsic properties of hemoglobin itself. Additionally, the genetic structure of hemoglobin, unless mutated, remains constant and does not affect its affinity.
How does increased pH effect oxygen levels?
Increased pH can lead to a decrease in oxygen levels as it can hinder the ability of hemoglobin to release oxygen to tissues in the body. This is known as the Bohr effect, where higher pH reduces the affinity of hemoglobin for oxygen, making it harder for oxygen to be released to tissues.
The highest oxygen affinity is demonstrated by?
The highest oxygen affinity is demonstrated by fetal hemoglobin (HbF), due to its higher affinity for oxygen compared to adult hemoglobin (HbA). This allows for efficient oxygen transfer from the mother to the fetus in the placenta.
Who is researching methemoglobinemia?
This is a congenital hemoglobinopathy where the hemoglobin has an increased affinity for oxygen, and therefore, it does not releases it to the tissues. The consequence is hypoxia, and clinically, the baby has a bluish to grey color. It is incompatible with life.
What is the relationship between pH and hemoglobin saturation?
The relationship between pH and hemoglobin saturation is known as the Bohr effect. When pH levels decrease (become more acidic), hemoglobin's affinity for oxygen decreases, leading to lower hemoglobin saturation. Conversely, when pH levels increase (become more basic), hemoglobin's affinity for oxygen increases, resulting in higher hemoglobin saturation.
Why does the rise in temperature decrease the affinity of hemoglobin for oxygen?
The rise of temperature denatures the bond between oxygen and hemoglobin.
What will decrease the affinity of hemoglobin for oxygen?
Factors that can decrease the affinity of hemoglobin for oxygen include an increase in temperature, a decrease in pH (acidity), an increase in levels of carbon dioxide, and the presence of certain substances like 2,3-DPG.
Shift in oxygen-Hb dissociation curve to the right the affinity of hemoglobin for oxygen?
As it shifts to the right, it means that haemoglobin has a lesser affinity for oxygen
Does a low pH decrease hemoglobins affinity for oxygen?
Yes, a low pH (acidic environment) decreases hemoglobin's affinity for oxygen. This is known as the Bohr effect, where pH and carbon dioxide levels affect oxygen-hemoglobin binding. In an acidic environment, hemoglobin releases oxygen more readily to tissues where it is needed.
