Affinity purification and structural characterization of a specific binding protein for human growth hormone in human serum.

摘要: Summary A highly specific binding protein for human growth hormone (hGH) has been isolated from serum by hGH-affinity chromatography. purification of ∼1500-fold with a 30–40% recovery was obtained essentially no alteration in characteristics. Covalent cross-linking 125I-hGH to the protein, followed analysis SDS-polyacrylamide gel electrophoresis and autoradiography, revealed two specifically labeled complexes. Allowing 1:1 stoichiometry proteins themselves had mean mol wts 57000 69300. These increased slightly wt 60300 72000 respectively presence 100 mM dithiothreitol, suggesting intramolecular but not inter-subunit disulfide linkages. data confirm hGH protein(s) define their gross structural nature.