| Autor: |
Reddy, Anthony, Grimwood, Brian G., Plummer, T.H., Tarentino, Anthony L. |
| Zdroj: |
Glycobiology; Jun1998, Vol. 8 Issue 6, p633-636, 4p |
| Abstrakt: |
The Endo F2 gene was overexpressed in E.coli as a fusion protein joined to the maltose‐binding protein. MBP‐Endo F2 was found in a highly enriched state as insoluble, inactive inclusion bodies. Extraction of the inclusion bodies with 20% acetic acid followed by exhaustive dialysis rendered the fusion protein active and soluble. MBP‐Endo F2 was digested with Factor Xa and purified on Q‐Sepharose. The enzyme was homogeneous by SDS–PAGE, and appeared as a single symmetrical peak on HPLC. Analysis of the amino‐terminus demonstrated conclusively that recombinant Endo F2 was homogeneous and identical to the native enzyme. [ABSTRACT FROM PUBLISHER] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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