| Literature DB >> 9219334 |
M Tokunaga1, M Ishibashi, D Tatsuda, H Tokunaga.
Abstract
We constructed two mouse alpha-amylase secretion vectors for Kluyveromyces lactis using the well-characterized signal sequence of the pGKL 128 kDa killer precursor protein. Both PHO5 and PGK expression cassettes from Saccharomyces cerevisiae directed the expression of mouse alpha-amylase in YPD medium at a similar level of efficiency. K. lactis transformants secreted glycosylated and non-glycosylated alpha-amylase into the culture medium and both species were enzymatically active. The K. lactis/S. cerevisiae shuttle secretion vector pMI6 was constructed, and K. lactis MD2/1(pMI6) secreted about four-fold more alpha-amylase than S. cerevisiae YNN27 harboring the same plasmid, indicating that K. lactis is an efficient host cell for the secretion and production of recombinant proteins.Entities:
Mesh：
Substances：
Year: 1997 PMID： 9219334 DOI： 10.1002/(SICI)1097-0061(19970630)13:8<699::AID-YEA124>3.0.CO;2-N
Source DB: PubMed Journal: Yeast ISSN： 0749-503X Impact factor: 3.239