Hemoglobina Flashcards
(26 cards)
What is hemoglobin?
Hemoglobin is a protein in red blood cells responsible for transporting oxygen from the lungs to the body’s tissues and returning carbon dioxide from the tissues back to the lungs.
What is the primary structure of hemoglobin composed of?
The primary structure of hemoglobin is composed of four polypeptide chains: two alpha chains and two beta chains.
True or False: Hemoglobin can bind to carbon dioxide.
True
What is the main function of hemoglobin?
The main function of hemoglobin is to carry oxygen from the lungs to the tissues and facilitate the return of carbon dioxide from the tissues to the lungs.
Fill in the blank: Hemoglobin contains a heme group that binds to ______.
oxygen
What is the significance of the iron ion in hemoglobin?
The iron ion in the heme group is essential for binding oxygen, as it can exist in a ferrous state (Fe2+) that can coordinate with oxygen.
What type of hemoglobin is present in fetal development?
Fetal hemoglobin (HbF), which has a higher affinity for oxygen than adult hemoglobin.
Which hemoglobin variant is associated with sickle cell disease?
Hemoglobin S (HbS)
What is the quaternary structure of hemoglobin?
The quaternary structure of hemoglobin refers to its assembly of four polypeptide chains (two alpha and two beta) that form a functional protein.
Multiple Choice: What is the typical concentration of hemoglobin in adult males?
15-17 g/dL
True or False: Hemoglobin can exist in a T (tense) and R (relaxed) state.
True
What role does 2,3-Bisphosphoglycerate (2,3-BPG) play in hemoglobin function?
2,3-BPG decreases hemoglobin’s affinity for oxygen, facilitating oxygen release in tissues.
What is the difference between hemoglobin A and hemoglobin A2?
Hemoglobin A (HbA) is the normal adult hemoglobin, while hemoglobin A2 (HbA2) is a minor component composed of two alpha and two delta chains.
Identify the type of hemoglobin that is formed due to a genetic mutation in the beta-globin gene.
Hemoglobin S (HbS), which causes sickle cell disease.
What is the physiological significance of hemoglobin’s cooperative binding?
Cooperative binding allows hemoglobin to pick up oxygen more efficiently in the lungs and release it more readily in tissues.
Fill in the blank: Hemoglobin’s ability to carry carbon dioxide is mainly through the formation of ______.
carbamino compounds
What is methemoglobin?
Methemoglobin is a form of hemoglobin in which the iron is in the ferric state (Fe3+) and cannot bind oxygen.
Multiple Choice: Which condition is characterized by a deficiency of hemoglobin?
Anemia
True or False: Hemoglobin can be affected by pH levels in the blood.
True
What is the role of myoglobin in comparison to hemoglobin?
Myoglobin is a protein that stores oxygen in muscle tissues, while hemoglobin transports oxygen in the blood.
What is the effect of carbon monoxide on hemoglobin?
Carbon monoxide binds to hemoglobin with a much higher affinity than oxygen, preventing oxygen transport.
What are the two main types of adult hemoglobin?
Hemoglobin A (HbA) and Hemoglobin A2 (HbA2).
Fill in the blank: The binding of oxygen to hemoglobin is an example of ______ binding.
allosteric
What is the Bohr effect?
The Bohr effect describes how increased levels of carbon dioxide and decreased pH promote oxygen release from hemoglobin.
