Korean Journal of Microbiology (미생물학회지)

The Microbiological Society of Korea (한국미생물학회)
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The Glucoamylase Signal Sequence Directs the Efficient Secretion of Human $\alpha$1-Antitrypsin in Yeast Cells

효모에서 Glucoamylase 신호서열에 의한 인체 $\alpha$1-Antitrypsin의 분비 효율 향상

  • Song, Moo-Young (Department of Microbiology, College of Natural Science, Chungnam National University) ;
  • Kwon, Ki-Sun (Genetic Engineering Research Institute, KIST) ;
  • Kang, Dae-Ook (Genetic Engineering Research Institute, KIST) ;
  • Yu, Myeong-Hee (Genetic Engineering Research Institute, KIST) ;
  • Park, Hee-Moon (Department of Microbiology, College of Natural Science, Chungnam National University) ;
  • Kim, Jinmi (Department of Microbiology, College of Natural Science, Chungnam National University)
  • Published : 1993.06.01
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Abstract

Five different secretion vectors were constructed by varying the signal sequences and .alpha.-antitrypsin (.alpha.1-AT) a numan secretory protein, was produced from yeast cells. The signal sequences used are those of acid phosphatase (PH05) and .alpha.-factor (M f.alphal1) of Saccharomyces cerevisiae, glucoamylase (STA1) of Saccharomyces diastaticus, and human .alpha.1-AT. Four vectors directed the efficient secretion of .alpha.1-AT ito the culture media. The secretion vector carrying the glucoamylase signal sequence (pGAT11) showed the highest efficiency of secretion. About 70% of .alpha.1-AT produce dwere secreted into the media. The endo H treatment of partially purified .alpha.1-AT indicates that the secreted .alpha.1-AT appeared to be glycosylated. This glycosylation pattern was altered when amino acid substitution mutations were introduced at the three glycosylation sites of .alpha.-AT.

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