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Amino Terminal Acetylation of Authentic Human Cu,Zn Superoxide Dismutase Produced in Yeast

Bio/Technology volume 5, pages 363–366 (1987)Cite this article

Abstract

Human Cu,Zn superoxide dismutase (HSOD) is an Nα–acetylated enzyme, which may be useful in the prevention of post–ischemic damage. Since HSOD expressed in E. coli is not Nα–acetylated we have investigated expression and Nα–acetylation in yeast. HSOD has been expressed at very high levels in yeast utilizing the yeast glyceraldehyde phosphate dehydrogenase promoter. It is soluble, of normal specific activity and confers low level resistance to copper and zinc. The yeast HSOD is acetylated at its N–terminus indicating that yeast cells may be useful for the production of Nα–acetylated proteins.

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Author notes

  1. Robert A. Hallewell: Corresponding author.

  2. Fritz Ötting: Grünenthal GmbH, Forschungszentrum Aachen-Eilendorf, Abteilung Proteinchemie.

Authors and Affiliations

  1. Chiron Corporation, 4560 Horton Street, Emeryville, CA, 94608

    Robert A. Hallewell, Robert Mills, Patricia Tekamp-Olson, Russel Blacher, Steven Rosenberg, Fritz Ötting, Frank R. Masiarz & Carl J. Scandella

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Hallewell, R., Mills, R., Tekamp-Olson, P. et al. Amino Terminal Acetylation of Authentic Human Cu,Zn Superoxide Dismutase Produced in Yeast. Nat Biotechnol 5, 363–366 (1987). https://doi.org/10.1038/nbt0487-363

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