A Quantitative Study of the Hydrolysis of Human Dinitrophenyl(DNP)globin: The Number and Kind of Polypeptide Chains in Normal Adult Human Hemoglobin
Abstract
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.
Additional Information
© 1957 American Chemical Society. Received April 11, 1957. This investigation was supported in part by a grant from the Ford Foundation and in part by a research grant (RG-4276(C)) from the National Institutes of Health, Public Health Service.Additional details
- Eprint ID
- 88266
- DOI
- 10.1021/ja01574a028
- Resolver ID
- CaltechAUTHORS:20180725-111211357
- Ford Foundation
- RG-4276(C)
- NIH
- Created
-
2018-07-25Created from EPrint's datestamp field
- Updated
-
2021-11-16Created from EPrint's last_modified field
- Other Numbering System Name
- Gates and Crellin Laboratories of Chemistry
- Other Numbering System Identifier
- 2199