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Research Papers
Bio/Technology  5, 363 - 366 (1987)
doi:10.1038/nbt0487-363

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

Robert A. Hallewell1, *, Robert Mills1, Patricia Tekamp-Olson1, Russel Blacher1, Steven Rosenberg1, Fritz Ötting1, , Frank R. Masiarz1 & Carl J. Scandella1

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

  *Corresponding author.

  Grünenthal GmbH, Forschungszentrum Aachen-Eilendorf, Abteilung Proteinchemie.

Human Cu,Zn superoxide dismutase (HSOD) is an Nalpha−acetylated enzyme, which may be useful in the prevention of post−ischemic damage. Since HSOD expressed in E. coli is not Nalpha−acetylated we have investigated expression and Nalpha−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 Nalpha−acetylated proteins.

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