Expression and purification of human angiotensinogen in Chinese hamster ovary cells

Biochim Biophys Acta. 1992 Jun 24;1121(3):335-8. doi: 10.1016/0167-4838(92)90166-b.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensinogen / biosynthesis
  • Angiotensinogen / genetics*
  • Angiotensinogen / isolation & purification
  • Animals
  • Blotting, Northern
  • CHO Cells
  • Chromatography, Liquid
  • Cloning, Molecular
  • Cricetinae
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Molecular Sequence Data
  • RNA, Messenger / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Renin / metabolism
  • Substrate Specificity

Substances

  • RNA, Messenger
  • Recombinant Proteins
  • Angiotensinogen
  • Renin