title: pH-dependent inactivation and reactivation of recombinant sheep angiotensinogen.
abstract: Purified recombinant sheep angiotensinogen (rsAngn) lost 74% of the reactivity with human renin during storage at pH 8.0 and 4 degrees C. The inactivated rsAngn was reactivated by incubation at acidic pHs. This indicates that pH-dependent inactivation and reactivation occur in rsAngn.
authors.affiliation: United Graduate School of Agricultural Sciences, Faculty of Agriculture, Gifu University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Nagase
authors.forename: F
authors.initials: F
authors.lastname: Suzuki
authors.forename: A
authors.initials: A
authors.lastname: Takahashi
authors.forename: M
authors.initials: M
authors.lastname: Fujimori
authors.forename: Y
authors.initials: Y
authors.lastname: Sawai
authors.forename: Y
authors.initials: Y
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D000808:Angiotensinogen / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D012083:Renin / Q000378:metabolism; D012756:Sheep
chemical_list: D010446:Peptide Fragments; D011994:Recombinant Proteins; D000808:Angiotensinogen; D012083:Renin