| Title | The Glucoamylase Gignal Gequence Girects the Gfficient Secretion of Human α1-Antitrypsin in Yeast Cells | ||
| Author | Song, Moo Young · Kwon, Ki Sun1 · Kang, Dae Ook1 · Yu, Myeong Hee1 · Park, Hee Moon · Kim, Jin Mi * | ||
| Address | Department of Microbiology, College of Natural Science, Chungnam National University; 1Genetic Engineerinf Researcj Institute, KIST | ||
| Bibliography | Korean Journal of Microbiology, 31(3),203-207, 1993 | ||
| DOI | |||
| Key Words | secretion, signal sequence, α1-AT, glucoamylase | ||
| Abstract | Five different secretion vectors were constructed by varying the signal sequences and α-antitrypsin (α1-AT) a numan secretory protein, was produced from yeast cells. The signal sequences used are those of acid phosphatase (PH05) and α-factor (Mfα1) of Saccharomyces cerevisiae, glucoamylase (STA1) of Saccharomyces diastaticus, and human α1-AT. Four vectors directed the efficient secretion of α1-AT ito the culture media. The secretion vector carrying the glucoamylase signal sequence (pGAT11) showed the highest efficiency of secretion. About 70% of α1-AT produce dwere secreted into the media. The endo H treatment of partially purified α1-AT indicates that the secreted α1-AT appeared to be glycosylated. This glycosylation pattern was altered when amino acid substitution mutations were introduced at the three glycosylation sites of α1-AT. | ||
| Download PDF | Kor_310305_203-207p0.pdf | ||