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The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer.

HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys

HbS: Val-His-Leu-Thr-Pro-Val-Glu-Lys

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batolisis

Yes The two peptides will separate from each other in an electric field when the pH is 7.0

The two peptides wil drift/separate from each other when the pH is 7.0 because of the reaction of trypsin enzyme and also the difference in charge between HbA and Hbs

Considering charge of each peptide

Since The isoelectric point of normal Hba is 6.9 and Hbs possess two fewer negative charges per hemoglobin molecules

The Hbs is more hydrophobicity than HbA due to the substitution of glutamic acids of HbS by valine residue.

Considering Electrophoresis

At a lower pH level Hbs shows a slower moving band than Hba

while a higher pH level the HbS peptide is less negatively charged while the carboxyl group of HbA is more negatively charged and Hba moves faster as well as an acidic pH.

Hence we can conclude that the two peptides will separate from each other in an electric field when the pH is 7.0

Learn more about peptides : https://brainly.com/question/17089864

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