Practice Quiz About Sickle Cell Disease

The S allele confers resistance to malaria because in low oxygen conditions, the cells containing the S allele sickle and eventually burst, disrupting the lifecycle of the malaria parasite. This disruption prevents the parasite from multiplying and causing the disease.

Hemoglobin is indeed found in the red blood cells and plays a crucial role in transporting oxygen and carbon monoxide throughout the body. It binds to oxygen in the lungs and carries it to tissues and organs, ensuring proper oxygenation. Additionally, hemoglobin can also bind to carbon monoxide, which is a harmful gas produced by combustion, preventing it from binding to other molecules and causing harm. Therefore, the statement "Hemoglobin is found in the red blood cells and carries oxygen and carbon monoxide from one area of the body to another" is true.

Hydroxyurea is indeed used to treat fetal hemoglobin. Fetal hemoglobin is a type of hemoglobin that is present in newborns and infants. It is different from adult hemoglobin and has a higher affinity for oxygen. Hydroxyurea is a medication that can stimulate the production of fetal hemoglobin in adults with certain blood disorders, such as sickle cell disease and beta-thalassemia. By increasing the levels of fetal hemoglobin, hydroxyurea can help to improve the symptoms and complications associated with these conditions. Therefore, the statement is true.

Each red blood cell contains approximately 270 million hemoglobin molecules. Hemoglobin is a protein found in red blood cells that carries oxygen from the lungs to the rest of the body. The high number of hemoglobin molecules in each red blood cell allows for efficient oxygen transport throughout the body.

The given statement is false. There is no evidence to suggest that the molecular basis behind SCD (Sickle Cell Disease) was found during Linus Pauling's famous light experiment. Linus Pauling was a renowned scientist known for his work on the nature of chemical bonds and his contributions to the field of molecular biology, but there is no direct connection between his experiments and the discovery of the molecular basis of SCD.

This statement is false because sickling of cells is directly related to the abnormal shape of red blood cells caused by the presence of abnormal hemoglobin. Sickle cell disease is a genetic disorder where the red blood cells contain abnormal hemoglobin, causing them to become rigid and sickle-shaped. Without the presence of abnormal hemoglobin, the cells would not sickle. Therefore, hemoglobin is necessary for cells to sickle in sickle cell disease.

Patients with sickle cell disease have an increased risk of infections due to the abnormal shape of their red blood cells. The misshapen cells can get stuck in blood vessels, leading to reduced blood flow and oxygen supply to tissues, making them more susceptible to infections. Penicillin, an antibiotic, is given to these patients as a prophylactic measure to prevent bacterial infections, particularly those caused by Streptococcus pneumoniae. By reducing the risk of infections, penicillin helps in managing the complications associated with sickle cell disease.

Hemoglobin is a molecule made up of polypeptides called alpha globin and beta globin. These two polypeptides combine together to form the complete hemoglobin molecule. Hemoglobin is responsible for carrying oxygen from the lungs to the tissues and removing carbon dioxide from the tissues back to the lungs. The presence of both alpha globin and beta globin is crucial for the proper functioning of hemoglobin.

The difference between AA and SS is the 9th amino acid of the beta globin polypeptide.

The genotype SA confers resistance to malaria. Sickle cell trait is caused by the presence of one normal hemoglobin gene (A) and one sickle hemoglobin gene (S). This combination provides some protection against malaria, as the parasite responsible for malaria cannot survive as easily in red blood cells with sickle hemoglobin. Therefore, individuals with the SA genotype have a reduced risk of contracting malaria compared to those with other genotypes.

Protease is the correct answer because it is an enzyme that specifically breaks down peptide bonds, which are the bonds that hold amino acids together in a protein chain. Protease enzymes play a crucial role in various biological processes, including digestion, protein turnover, and cell signaling. They are responsible for breaking down proteins into smaller peptides and amino acids, allowing for their absorption and utilization by the body. Therefore, protease is the enzyme that destroys peptide bonds.

The statement suggests that the SA allele is not very common in the African highlands.

2-D electrophoresis is a technique used to separate and analyze proteins based on their charge and size. In the context of sickle cell disease, this method was used to identify the abnormal hemoglobin protein responsible for the disease. By subjecting the hemoglobin samples from individuals with sickle cell disease to 2-D electrophoresis, researchers were able to observe a distinct band corresponding to the mutated hemoglobin protein. This provided evidence for the molecular basis of sickle cell disease, demonstrating that a specific mutation in the hemoglobin gene leads to the production of abnormal hemoglobin proteins.

Red blood cells need a specific protein called hemoglobin in order for them to sickle. Hemoglobin is responsible for carrying oxygen throughout the body. In individuals with sickle cell disease, a genetic mutation causes the hemoglobin to form abnormal shapes, leading to the characteristic sickle shape of the red blood cells. This altered hemoglobin causes the cells to become rigid and prone to getting stuck in blood vessels, resulting in various complications.

Dantu blood group has an extra layer of carbohydrates that acts as a protective shield against the malaria parasite. This additional layer prevents the parasite from entering the blood cells, reducing the risk of infection.