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Quantitative study examines hydrolysis effects on hemoglobin, revealing polypeptide chain structures and residues.
A quantitative investigation of the partial hydrolysis of DNP-globin in refluxing 6 N hydrochloric acid has led to an explanation of our earlier conclusion that normal adult human hemoglobin contains a non-integral number, 3.6, of N-terminal valyl residues per molecule. It is now concluded that 4 E-terminal residues are present. Moreover, it has been found that the molecule contains two kinds of polypeptide chains, with respect to the K-termini. Under the above hydrolytic conditions the N-terminal valyl residues are released as DNP-Val-leu almost quantitatively from two chains (A chains) within 15 min. On continued hydrolysis the other two chains (B chains) release DNP-valine. No N-terminal peptides originating from the B chains have been definitely identified.
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Rhinesmith et al. (1957) studied this question.
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