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#red blood cells

26 public questions tagged with this topic.

Which is the major site of production of red blood lls in adults?

In adults, red blood lls are primarily produced in the bone marrow. This follows from NCERT principle where the relation explains the outcome clearly for students in simple steps.

Ref: NCERT Biology Textbook for Class XI and XII (Zoology section), Chapter: Structural Organisation in Animals and Frog, Topic: Tissues, skeletal and organ systems.

Which RBC membrane protein is essential for Cl⁻ transport?

Physiology of carbon dioxide delivery relies on chloride bicarbonate exchange across erythrocyte membrane rather than G protein signaling. Authentic transporter Band 3 anion exchanger 1 SLC4A1 abundant integral protein fourteen transmembrane helices catalyzing electroneutral one to one antiport of chloride for bicarbonate at high turnover supporting conversion of CO2 to bicarbonate via carbonic anhydrase for plasma carriage known as chloride shift Hamburger phenomenon. At pulmonary capillaries exchange reverses enabling CO2 exhalation. GPCR family members are seven-transmembrane receptors coup

Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 15, AE1 Band 3 Chloride-Bicarbonate Exchanger.

Which protein is responsible for maintaining the biconcave shape of RBCs?

Maintenance of biconcave disc shape maximizing surface to volume ratio for deformability and gas exchange depends on membrane skeleton elasticity and organization. Spectrin consists of alpha two hundred eighty kilodalton and beta two hundred forty six kilodalton subunits each containing twenty triple-helical spectrin repeats of one hundred six residues forming elongated flexible anti-parallel heterodimer one hundred nanometers long, two heterodimers associate head to head via helical bundle forming tetramer about two hundred nanometers acting as entropic spring with persistence length about te

Ref: Lux and Palek, Erythrocyte Membrane Skeleton and Spectrin Elasticity, Blood Cells.

Which statement about Glycophorin A is correct?

Detailed topology of glycophorin A major human erythrocyte sialoglycoprotein clarifies single-pass characteristics. Gene GYPA on chromosome four encodes one hundred fifty residues including cleavable signal peptide. Mature protein seventy kilodalton apparent due to extensive glycosylation: seventy residue extracellular domain heavily O-glycosylated fifteen O-linked tetrasaccharides NeuAc alpha2-3 Gal beta1-3 GalNAc plus one N-linked complex chain adding sialic acid dense negative charge defining MNS blood group M and N antigens and preventing rouleaux formation. Hydrophobic anchor residues sev

Ref: Alberts et al., Molecular Biology of the Cell, 6th ed., Chapter 10, Glycophorin A Structure and Topology.

What happens when red blood cells are placed in a hypotonic solution?

Human erythrocytes are discoid cells lacking nucleus and organelles, bounded by lipid bilayer containing aquaporin-1 water channels and Band 3 anion exchanger, supported by spectrin-actin cytoskeleton providing elasticity but limited capacity to expand. Cytoplasm osmolarity about 300 milliosmoles dominated by potassium, chloride and hemoglobin remains nearly isotonic with plasma. Placing these cells into hypotonic solution where extracellular solute osmolarity lower than intracellular creates higher extracellular water chemical potential. Water rapidly enters down gradient via aquaporin-1 at b

Ref: Guyton and Hall, Textbook of Medical Physiology, Chapter 4: Erythrocyte Osmosis and Hemolysis in Hypotonic Solutions.