Table of pK_as for standard amino acids Another mutation in hemoglobin has been
ID: 174051 • Letter: T
Question
Table of pK_as for standard amino acids Another mutation in hemoglobin has been discovered. The glutamic add residue in the 6m position in the beta-chain has been replaced with a lysine residue. Is it possible to diagnose this abnormal hemoglobin, Hb X, by electrophoresis at pH 9.2? Explain your answer in detail, indicating how you would (or would not) be able to distinguish between Hb A (normal), Hb S (side cell), and Hb X (Newly discovered). Use pKas and how the net charge changes with pH and use diagrams if necessary.Explanation / Answer
HbS contains valine in place of glutamic corrosive in the sixth amino corrosive position of the beta subunit. This advances hydrophobic connection among Hb particles and results in polymerization of the HbS atoms and RBC bending.
HbC is brought about by a solitary amino corrosive substitution (lysine rather than glutamic corrosive at position 6 in the beta globin chain in the Hb atom.
HbA-NORMAL
HbS---------ABNORMAL -CAN BE DIAGNOSED
Hb X--------ABNORMAL hemoglobin MAY HAVE SIMILAR FEATURES THAT OF HbC.
even though hemoglobin X is a mutant form of hemoglobin .
Hb X-- will not polymerize as hemoglobin S does
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