| Literature DB >> 390363 |
Abstract
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 porperties. 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 COOH-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.Entities:
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Year: 1979 PMID: 390363 DOI: 10.1007/bf00849278
Source DB: PubMed Journal: Mol Cell Biochem ISSN: 0300-8177 Impact factor: 3.396