Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes.

@article{Wei1991ExpressionAC,
  title={Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes.},
  author={L. Wei and F. Alhenc-Gelas and F. Soubrier and A. Michaud and P. Corvol and E. Clauser},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 9},
  pages={
          5540-6
        }
}
Chinese hamster ovary (CHO) cells have been transfected with either a full-length cDNA encoding human angiotensin I-converting enzyme (kininase II; EC 3.4.15.1) (ACE) or a mutated cDNA, in which the last C-terminal 47 amino acids, including the putative transmembrane domain, are not translated. Cell lines expressing high levels of the wild-type ACE or the mutant were established. The cells transfected with the wild-type cDNA (CHO-ACE) express a membrane-bound ectoenzyme with an intracellular C… Expand
Cleavage-secretion of angiotensin I-converting enzyme in yeast
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