bis102-10-17-lec11

bis102-10-17-lec11 - 10/17/2011 Fetal hemoglobin- tetramer...

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10/17/2011 Fetal hemoglobin- tetramer containing 2 alpha chains and 2 gamma chains The gamma chain has 72% identity in amino acid sequence with the beta-chain. this difference in sequence does not enable fetal hemoglobin to bind to 2,3 -BPG as well as adult hemoglobin and as a result the fetal hemoglobin has a higher affinity for oxygen than maternal hemoglobin. The mother can thus transport oxygen from her hemoglobin to the fetus hemoglobin. -enables fetus to be rich in oxygen. Detrimental mutations of hemoglobin genes -about 7% of the world population carry disorders in sequence of hemoglobin genes. ex: sickle cell anemia - single substitution of a glutamate residue at position 6 of the beta-subunit with valine produces a mutated form called hemoglobin S. valine is hydrophobic-- it ends up binding with hydrophobic residues of other hemoglobin residues. .. the hemoglobin starts to aggregate together. to have sickle cell - must have mutation in both alleles of the gene for the beta-chain.
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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bis102-10-17-lec11 - 10/17/2011 Fetal hemoglobin- tetramer...

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