Abstract:
:The Endo F2gene was overexpressed in E.coli as a fusion protein joined to the maltose-binding protein. MBP-Endo F2was 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 F2was digested with Factor Xaand 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 F2was homogeneous and identical to the native enzyme.
journal_name
Glycobiologyjournal_title
Glycobiologyauthors
Reddy A,Grimwood BG,Plummer TH,Tarentino ALdoi
10.1093/glycob/8.6.633subject
Has Abstractpub_date
1998-06-01 00:00:00pages
633-6issue
6eissn
0959-6658issn
1460-2423pii
cwb068journal_volume
8pub_type
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