Expression and purification of human angiotensinogen in Chinese hamster ovary cells.
We have produced human angiotensinogen in Chinese hamster ovary (CHO) cells. The expression products were purified to homogeneity by a single column chromatography and its 17 amino-terminal sequences were identical to those of the native protein. We demonstrated the recombinant human angiotensinogen to be a substrate for human renin.
Hatae
T
T
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Takimoto
E
E
Fukamizu
A
A
Hori
H
H
Kimoto
K
K
Murakami
K
K
D000595:Amino Acid Sequence; D000808:Angiotensinogen / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D000818:Animals; D015152:Blotting, Northern; D016466:CHO Cells; D002853:Chromatography, Liquid; D003001:Cloning, Molecular; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D012083:Renin / Q000378:metabolism; D013379:Substrate Specificity
D012333:RNA, Messenger; D011994:Recombinant Proteins; D000808:Angiotensinogen; D012083:Renin