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- W1973103437 abstract "The effects of glycosylation on stability and activity of recombinant cystatin were investigated using two yeast expression systems. A great difference in the length of polymannosyl chains in addition to 2 mol of N-acetylglucosamine was observed in mouse cystatin C produced by Saccharomyces cerevisiae and Pichia pastoris transformants. Polymannosylated cystatin with degree of polymerization (DP) of 310 (Cyst310) was predominantly produced by S. cerevisiae as a heterogeneous glycoprotein. In contrast, the DP of cystatin by P. pastoris was 90 (Cyst90). These yeast transformants also produced a small amount of oligomannosylated cystatin with DP of 13 (Cyst13) as well as unglycosylated protein. Susceptibility of Cyst310 and Cyst90 to α-chymotrypsin dramatically decreased to <10%, while that of Cyst13 was 77% of the susceptibility of unglycosylated cystatin. Polymannosylation improved the heat stability of cystatin to an extent that no coagulation was observed under the conditions, which coagulated unglycosylated protein. Papain-inhibiting activities of Cyst310, Cyst90, and Cyst13 were 18.5, 83.7, and 98.3% of that of unglycosylated cystatin, respectively. The retentions of inhibitory activity upon heating to 95 °C were 82.2 and 71.3% for Cyst310 and Cyst90, respectively, while those of Cyst13 and unglycosylated cystatin were below 10%. The polymannosylation of cystatin by P. pastoris is preferable to that by S. cerevisiae as the resulting protein is more stable and active in inhibiting papain. Keywords: Mouse cystatin C; Saccharomyces cerevisiae; Pichia pastoris; polymannosylation; protease susceptibility; heat stability" @default.
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- W1973103437 date "1998-06-03" @default.
- W1973103437 modified "2023-10-18" @default.
- W1973103437 title "Effects of Polymannosylation of Recombinant Cystatin C in Yeast on Its Stability and Activity" @default.
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- W1973103437 doi "https://doi.org/10.1021/jf9801217" @default.
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