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Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity.

Abstract:

Using site directed mutagenesis combined with chemical modification, we have developed a general and versatile method for the glycosylation of proteins which is virtually unlimited in the scope of proteins and glycans that may be conjugated and in which the site of glycosylation and the nature of the introduced glycan can be carefully controlled. We have demonstrated the applicability of this method through the synthesis of a library of 48 glycosylated forms of the serine protease subtilisin ...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Journal:
Bioorganic and medicinal chemistry
Volume:
8
Issue:
7
Pages:
1537-1544
Publication date:
2000-07-01
DOI:
EISSN:
1464-3391
ISSN:
0968-0896
Source identifiers:
52044
Language:
English
Keywords:
Pubs id:
pubs:52044
UUID:
uuid:1fb98ec8-5484-4863-8665-a4015c68a265
Local pid:
pubs:52044
Deposit date:
2012-12-19

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