The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding

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Neena Din ◽  
Ian J. Forsythe ◽  
Leslie D. Burtnick ◽  
Neil R. Gilkes ◽  
Robert C. Miller ◽  
...  
1996 ◽  
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Mark R. Bray ◽  
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R. Antony J. Warren ◽  
Lawrence P. Mcintosh ◽  
...  

1993 ◽  
Vol 106 (1) ◽  
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Geoffrey P. Hazlewood ◽  
Neville S. Huskisson ◽  
Richard Virden ◽  
Harry J. Gilbert

1989 ◽  
Vol 7 (6) ◽  
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Neil R. Gilkes ◽  
R. Antony J. Warren ◽  
Robert C. Miller ◽  
Douglas G. Kilburn

2013 ◽  
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Su-Lim Choi ◽  
Haseong Kim ◽  
Jung Hoon Sohn ◽  
Seung-Goo Lee

1999 ◽  
Vol 339 (2) ◽  
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R. Keith HUMPHRIES ◽  
R. Antony J. WARREN ◽  
...  

A chimaera of stem cell factor (SCF) and a cellulose-binding domain from the xylanase Cex (CBDCex) effectively immobilizes SCF on a cellulose surface. The fusion protein retains both the cytokine properties of SCF and the cellulose-binding characteristics of CBDCex. When adsorbed on cellulose, SCF–CBDCex is up to 7-fold more potent than soluble SCF–CBDCex and than native SCF at stimulating the proliferation of factor-dependent cell lines. When cells are incubated with cellulose-bound SCF–CBDCex, activated receptors and SCF–CBDCex co-localize on the cellulose matrix. The strong binding of SCF–CBDCex to the cellulose surface permits the effective and localized stimulation of target cells; this is potentially significant for long-term perfusion culturing of factor-dependent cells. It also permits the direct analysis of the effects of surface-bound cytokines on target cells.


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