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- W2393058887 abstract "Polypeptide∶N-acetylgalactosaminyl transferase (ppGalNAc-T) is the primary enzyme of O-glycosylation and plays an important role in forming O-polysaccharide. To investigate the functional and structure of the enzyme familiy further,the target DNA fragment enconding ppGalNAc-T2 was amplified from cloning plasmid pDONR201-T2 by PCR and sub-cloned into the prokaryotic expression vector pGEX-4T-1,the recombinant vector was introduced into E.coli BL21 for efficient expression. The GST-fusion protein was purified through GST-column. Analysis for the recombinant protein with Western blot showed a single band as expected.Using deduced ppGalNAc-T2 amino acid sequences in TBLAST search of human genomic DNA database identified several sequences,among them the highest homology was ricin-like domain,alignments between ppGalNAc-T2 and ricin-like domain were optimal in Swiss-PDB Viewer,finally examination with PROCHEK revealed that the molecular modeling of the enzyme has 91.4% of amino acid residues located in optimal region providing the O-glycosylation location." @default.
- W2393058887 created "2016-06-24" @default.
- W2393058887 creator A5042402553 @default.
- W2393058887 date "2005-01-01" @default.
- W2393058887 modified "2023-09-25" @default.
- W2393058887 title "Prokaryotic Expression,Purification of Human ppGalNAc-T2 and Structure Simulation for the Ricin-like Domain" @default.
- W2393058887 hasPublicationYear "2005" @default.
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