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Secretion of Mouse α-Amylase fromKluyveromyces lactis by MASAO TOKUNAGA; MATSUJIRO ISHIBASHI; DAISUKE TATSUDA; HIROKO TOKUNAGA is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Secretion of Mouse α-Amylase fromKluyveromyces lactis about?

We constructed two mouse -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 -amylase in YPD medium at a similar level of efficiency. K. lactis transformants secreted glycosylated and non-glycosylated -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 -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.

Who reads Secretion of Mouse α-Amylase fromKluyveromyces lactis?

Author

MASAO TOKUNAGA; MATSUJIRO ISHIBASHI; DAISUKE TATSUDA; HIROKO TOKUNAGA

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); John Wiley & Sons Inc.; [Chichester]; [New York]: John Wiley & Sons, ©1985-; Wiley; Hindawi Limited (ISSN 0749-503X)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)