title: Efficient production of recombinant human (pro)renin utilizing a decahistidine tag attached at the C-terminus.
abstract: Human prorenin attached by a decahistidine tag at the C-terminus was produced in Chinese hamster ovary cells. The tagged protein secreted into the culture medium was in the inactive prorenin form, and was activated to mature renin by proteolytic removal of its prosegment by trypsin in the same manner as native prorenin. The tagged (pro)renin was efficiently purified by metal-chelate affinity chromatography. The enzymatic properties of mature renin carrying the tag were similar to native renin. These results indicate that the introduction of a decahistidine tag at the C-terminus does not interfere with either the correct folding of prorenin or the catalytic activity of mature renin.
authors.affiliation: Laboratory of Applied Biochemistry, Faculty of Applied Biological Science, Gifu University, Japan. nakagawa@gifu-u.ac.jp
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Nakagawa
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Nishiuchi
authors.forename: Jyunji
authors.initials: J
authors.lastname: Akaki
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Iwata
authors.forename: Ryousuke
authors.initials: R
authors.lastname: Satou
authors.forename: Fumiaki
authors.initials: F
authors.lastname: Suzuki
authors.forename: Yukio
authors.initials: Y
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012083:Renin / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D012083:Renin