| Autor: |
Borsig, L., Ivanov, S.X., Herrmann, G.F., Kragl, U., Wandrey, C., Berger, E.G. |
| Zdroj: |
Biochemical and Biophysical Research Communications; May 1995, Vol. 210 Issue: 1 p14-20, 7p |
| Abstrakt: |
Expression of recombinant full length human α2,6(N)sialyltransferase has been scaled-up in S. cerevisiaein a 150-1 bioreactor yielding 47 U at a concentration of 0.31 U/l. The protein specific activity as measured in reconstituted yeast lyophilisate was 0.8 mU/mg protein. The recombinant enzyme exhibited similar Michaelis constants as previously determined for the native rat enzyme. By immunoblotting the enzyme was shown to be heterogeneous by size (44-48 kD) and N-glycosylated. We conclude that recombinant α2,6(N)sialyltransferase expressed in S. cerevisiaeis retained in the endoplasmic reticulum as a fully active enzyme. |
| Databáze: |
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