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Lookup NU author(s): Dr Deepan Shah,
Emeritus Professor Roy Russell
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Glucosyltransferase I (GTF-I) of Streptococcus downei synthesises an insoluble alpha-1,3-linked glucan from sucrose. It contains a catalytic domain that is a circularly-permuted homologue of the catalytic domain of Family 13 enzymes and a C-terminal glucan-binding domain (CBD) that consists of a series of tandem repeats, each similar to35 amino acids long. In order to examine the contribution of these repeats to binding, a nested series of plasmids was constructed that expressed truncated forms of GTF-I or GBD in Escherichia coli, with an N-terminal His(6) tag. The tag facilitated rapid purification and also allowed development of a novel microtitre tray assay in which binding of biotin-labelled dextran to immobilised GTF-I or GBD could be quantitatively determined. The capacity to bind dextran was proportional to the number of repeats, with a minimum of four repeats necessary to demonstrate binding in this assay.
Author(s): Russell RRB; Shah DSH
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: Biologia: 1st Symposium on the Alpha-Amylase Family
Year of Conference: 2002
Publisher: Slovak Academic Press Ltd.
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