Summary
The current status of the purification and characterization of human angiotensinogen is reviewed. One problem encountered in the past has been the copurification of a protein with similar properties. This protein has tentatively been designated alanine-protein. An efficient separation of angiotensinogen and alanine-protein was obtained on a zinc chelate column. Alanine-protein has been purified and its amino acid and carbohydrate composition determined. The COON-terminal amino acid and the NH2-terminal amino acid were determined to be serine and alanine, respectively. Alanine-protein exhibited multiple forms on isoelectric focusing.
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This work was supported in part by a Grant-in-Aid from the American Heart Association and with funds contributed in part by the Wisconsin Heart Association.
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Tewksbury, D.A., Dart, R.A. Human plasma angiotensinogen: A review of purification procedures. Mol Cell Biochem 27, 47–56 (1979). https://doi.org/10.1007/BF00849278
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DOI: https://doi.org/10.1007/BF00849278