A four-step method for the purification of human angiotensinogen has been devised. The four steps are: (1) removal of albumin by affinity chromatography on blue dextran-Sepharose, (2) chromatography on DEAE-Sephadex, (3) chromatography on hydroxylapatite, and (4) chromatography on DEAE-cellulose. This method is capable of producing 8 mg of purified angiotensinogen from 150 ml of plasma with 33% overall recovery of renin-releasable angiotensin I. The angiotensinogen appears homogeneous by immunochemical and ultracentrifugal techniques. The N-terminal amino acids have been determined to be alanine and aspartic acid or asparagine.