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Hemoglobin A has a pI = 6.9. A variant, hemoglobin M, has a residue of glutamate...

Hemoglobin A has a pI = 6.9. A variant, hemoglobin M, has a residue of glutamate at position 67 instead of valine. What effect does this replacement in electrophoretic behavior at pH 7.5?

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Answer #1

Facts

1) pI is the isoelectric point at which the peptide or protein doesnot move towards any electrode or is having no net charge. For a protein with more basic amino acids, pI will be high while for an acidic protein the pI will be lower.

2) A protein that is in a pH below its pI will be positively charged and will migrate towards the negatively charged cathode. A protein that is in a pH above its pI will be negatively charged and will migrate towards the positively charged anode.

NOW LETS SOLVE

At pH 6.9, hemoglobin A has no net charge so will not migrate towards any electrode

Above pH 6.9 i.e. 7.5 it will be negatively charged and will move towards anode.

In hemoglobin M, If we replace valine by glutamate, we are adding an acidic side group and removing a neutral side group. It will decrease the isoelectric point of the protein as glutamate side chain will lose its acidic proton before 7.5 pH. It will also move towards anode more quickly than hemoglobin A

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