Hemoglobin Analysis

Hemoglobin Analysis - Genetic Analysis of Hemoglobin...

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Genetic Analysis of Hemoglobin (adapted from EXP 102 by John N. Anderson, Modern Biology, Inc., West Lafayette, IN.) Content Skills 1. Describe the genetic and biochemical basis for differences in electrophoretic movement of wild type and mutant forms of the protein hemoglobin. 2. Explain the heterozygosity of hemoglobin at the organismal and molecular level. Process Skills 1. Apply micropipetting skills to gel electrophoresis. 2. Apply gel electrophoresis to the analysis of proteins. Introduction Hemoglobin (Hb), the oxygen transporting protein, is a globular protein made up of four subunits. Two of the four subunits are identical alpha chains, each with 141 amino acids. The remaining two chains are called beta chains, each with 146 amino acids. In humans, about one out of 100 will posses a mutant form of hemoglobin. Sickle cell anemia results in humans who have Hb with a single glutamic acid residue in the beta chain replaced by a valine. The single residue change results in a conformation change in the protein structure, and a less negative charge in certain buffers. Under oxygen- deficient conditions, the mutant sickle cell hemoglobin will crystallize, which distorts the shape of the RBC. These abnormal RBCs are rapidly destroyed, causing a deficiency of RBCs and hence less oxygen transport (anemia). The sickled cells can also clog
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Hemoglobin Analysis - Genetic Analysis of Hemoglobin...

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