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Correct in vivo processing of a chimeric ubiquitin-proapolipoprotein A-I fusion protein in baculovirus-infected insect cells

Authors
Journal
Journal of Biotechnology
0168-1656
Publisher
Elsevier
Publication Date
Volume
32
Issue
1
Identifiers
DOI: 10.1016/0168-1656(94)90118-x
Keywords
  • N-Terminal Methionine
  • Ubiquitin
  • Ubiquitin Hydrolase
  • Fusion Protein
  • Insect Cell Baculovirus
Disciplines
  • Biology

Abstract

Abstract The cDNA coding for human proapolipoprotein A-I was expressed as a ubiquitin fusion under the control of the polyhedrin promoter in baculovirus-infected Sf9 Spodoptera frugiperda insect cells. The fusion protein was expressed at high level and was quantitatively cleaved in vivo. The cleaved product was purified and its N-terminal amino acid sequence was established. The data showed that authentic proapolipoprotein A-I has been produced, and thus demonstrated the existence in Spodoptera frugiperda insect cells of a specific ubiquitin hydrolase activity.

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