title: Isolation of angiogenin from normal human plasma.
abstract: Angiogenin, a potent blood vessel inducing protein, was previously isolated from medium conditioned by a human adenocarcinoma cell line [Fett, J. W., Strydom, D.J., Lobb, R.R., Alderman, E.M., Bethune, J.L., Riordan, J.F., & Vallee, B.L. (1985) Biochemistry 24, 5480-5486]. We now report that a protein which is physically and functionally identical with angiogenin is present in normal human plasma and can be purified to homogeneity by CM 52 and Mono S cation-exchange chromatography. The plasma-derived angiogenin exhibits the same angiogenic and ribonucleolytic activities, amino acid composition, molecular weight, immunoreactivity, and chromatographic behavior as the tumor cell derived protein. Peptide mapping and sequencing studies indicate chemical identity of the two proteins. The present yield of angiogenin from either plasma or serum is 60-150 micrograms/L. These findings demonstrate that angiogenin is not a tumor-specific product and provide further opportunities for the investigation of the role and mechanism of action of angiogenin and its potential diagnostic or prognostic utility.
authors: Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, Massachusetts 02115.
authors: R
authors: R
authors: Shapiro
authors: D J
authors: DJ
authors: Strydom
authors: K A
authors: KA
authors: Olson
authors: B L
authors: BL
authors: Vallee
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D043925:Angiogenesis Inducing Agents / Q000097:blood*; D004797:Enzyme-Linked Immunosorbent Assay; D006133:Growth Substances / Q000097:blood*; D006801:Humans; D009363:Neoplasm Proteins / Q000097:blood* / Q000302:isolation & purification; D012259:Ribonuclease, Pancreatic
chemical_list: D000596:Amino Acids; D043925:Angiogenesis Inducing Agents; D006133:Growth Substances; D009363:Neoplasm Proteins; C046366:angiogenin; D012259:Ribonuclease, Pancreatic