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BCH210H1 (352)
Lecture 6

Lecture 6 Text Notes

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Stavroula Andreopoulos

Lecture 6 Text Notes 2,3-Bisphosphoglycerate - important allosteric effector for hemoglobin - binding of 2,3-BPG to Hb promotes the release of O 2 - ionic bonds between 2,3-BPG and two β-chains stabilize Hb in the deoxy conformation – favours the dissociation of oxygen - oxyhemoglobin – central cavity is too small for 2,3-BPG to fit – conformational changes in O binding prevent 2,3-BPG from reaching the 2 BPG-binding site - hemoglobin stripped of BPG is saturated with O and cann2t release the oxygen within tissues – BPG shifts the oxygen saturation curve of Hb to the right – Hb as an O d2livery system suited to the needs of the organism - fetal Hb is better able to absorb O tha2 maternal Hb – effective transfer of oxygen can occur Sickle-Cell Anemia - instead of the characteristic disc shape, erythrocytes are elongated and crescentlike in form - sickle cells pass less freely through capillaries – impair circulation and cause tissue damage - cells are more fragile and rupture more easily than normal red blood cells – leads to anemia - single amino acid substitution in the β-chains of Hb cause sickle-cell anemia – replacement of the glutamate residue at position 6 in the β-chain by a valine residue - only difference between Hb A and Hb S (sickle-cell hemoglobin) - aliphatic side chains of the Val residues in Hb S create hydrophobic protrusions - aggregation of Hb S molecules into long chainlike polymeric structures – deoxy Hb S is less soluble than deoxy Hb A Immunoglobulins - antibody response – B cells, T cells, macrophage - B cells – mature in the bone marrow - T cells – mature in the thymus gland - antibodies – immunoglobulin proteins secreted from B cells
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