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How much hemoglobin can a RBC carry?
Each red blood cell can carry approximately 270 million hemoglobin molecules. Hemoglobin is the protein responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs.
Which types of mutation causes sickle cell anemia?
Sickle cell anemia is caused by a point mutation in the HBB gene, specifically a substitution of adenine for thymine in the sixth codon of the gene, resulting in the production of abnormal hemoglobin known as hemoglobin S.
What is the molecular basis for the difference in the electrophoretic pattern between normal hemoglobin A and hemoglobin S?
The difference in electrophoretic pattern between normal hemoglobin A and hemoglobin S is due to a single amino acid substitution. In hemoglobin S, a glutamic acid is replaced by a valine at position 6 of the beta-globin chain. This change causes hemoglobin S to have a different charge, leading to its characteristic migration pattern on electrophoresis.
How does sickle cell hemoglobin differ from normal hemoglobin?
Sickle cell hemoglobin differs from normal hemoglobin due to a mutation in the gene that codes for the hemoglobin protein. This mutation leads to the production of an abnormal hemoglobin variant (HbS) that causes red blood cells to become sickle-shaped, leading to various complications such as blockages in blood vessels and reduced oxygen delivery to tissues.
Force that holds molecules of a single material together?
Cohesion
How much hemoglobin can a RBC carry?
Each red blood cell can carry approximately 270 million hemoglobin molecules. Hemoglobin is the protein responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs.
Which types of mutation causes sickle cell anemia?
Sickle cell anemia is caused by a point mutation in the HBB gene, specifically a substitution of adenine for thymine in the sixth codon of the gene, resulting in the production of abnormal hemoglobin known as hemoglobin S.
What is the molecular basis for the difference in the electrophoretic pattern between normal hemoglobin A and hemoglobin S?
The difference in electrophoretic pattern between normal hemoglobin A and hemoglobin S is due to a single amino acid substitution. In hemoglobin S, a glutamic acid is replaced by a valine at position 6 of the beta-globin chain. This change causes hemoglobin S to have a different charge, leading to its characteristic migration pattern on electrophoresis.
How does sickle cell hemoglobin differ from normal hemoglobin?
Sickle cell hemoglobin differs from normal hemoglobin due to a mutation in the gene that codes for the hemoglobin protein. This mutation leads to the production of an abnormal hemoglobin variant (HbS) that causes red blood cells to become sickle-shaped, leading to various complications such as blockages in blood vessels and reduced oxygen delivery to tissues.
Force that holds molecules of a single material together?
Cohesion
What type of mutations exist in sickle cell allele?
The sickle cell allele can have a point mutation where a single nucleotide is changed, resulting in the substitution of glutamic acid with valine in the beta-globin chain of hemoglobin. This leads to the characteristic sickle-shaped red blood cells in individuals with sickle cell disease.
How many heme groups are contained in one molecule of hemoglobin?
There are four hemes. So, theoretically, up to 4 oxygen molecules can bond to a single hemoglobin. However, in practice, this seldom occurs.(usually fewer)
How many molecules of hemoglobin in one red blood cell?
250 million X 4 = < 1 billion4- is how many o2 molecules a single HBn carries assuming they are full saturated(which they almost never are)Actually, one hemoglobin molecule can carry 4 molecules of oxygen. There are ~1 billion molecules of oxygen in each RED BLOOD CELL.
How does a single DNA molecule produce two identical molecules?
Two single chains bond together. The bonded chains twist together to form a double helix.
Difference of myoglobin and hemoglobin?
myoglobin: the molecule is compact there is no water inside it with the exception of a very small number(less than 5) of single water molecules presumably trapped at the time the molecules is folded up. hemoglobin: it iz 4 times larger than myoglobin. it is spherical molecule formed by 4 subunits which are identical in pairs . each subunits has a conformation closely resembling that of myoglobin and the aggregation is held together by extensive van der waals forces.
How is the structural effects that this point mutation has on the hemoglobin protein?
A point mutation in the hemoglobin gene can lead to a single amino acid substitution in the protein, potentially altering its structure and function. This change can affect the stability of the hemoglobin tetramer, impacting its ability to bind and release oxygen efficiently. For example, the well-known mutation causing sickle cell disease results in the substitution of valine for glutamic acid, leading to the formation of rigid, sickle-shaped red blood cells that can obstruct blood flow. Overall, such structural changes can significantly impair oxygen transport and lead to various health complications.
How many haem molecules are attached to a polypeptide chain?
Typically, a single polypeptide chain in a hemoglobin molecule can bind to 4 heme molecules. Each heme molecule contains an iron atom that can bind to an oxygen molecule for transport in the bloodstream.
