title: Human plasma angiotensinogen: a review of purification procedures.
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.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000808:Angiotensinogen / Q000097:blood / Q000302:isolation & purification*; D000809:Angiotensins / Q000302:isolation & purification*; D001798:Blood Proteins / Q000302:isolation & purification; D002241:Carbohydrates / Q000032:analysis; D002845:Chromatography / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007525:Isoelectric Focusing; D012083:Renin / Q000097:blood
chemical_list: D000596:Amino Acids; D000809:Angiotensins; D001798:Blood Proteins; D002241:Carbohydrates; D000808:Angiotensinogen; D012083:Renin