scholarly journals The Inhibitory Effect of an RGD-Human Chitin-Binding Domain Fusion Protein on the Adhesion of Fibroblasts to Reacetylated Chitosan Films

2008 ◽  
Vol 40 (3) ◽  
pp. 269-279 ◽  
Author(s):  
Vera Carvalho ◽  
Lucília Domingues ◽  
Miguel Gama
Keyword(s):  
Fusion Protein ◽  
Inhibitory Effect ◽  
Binding Domain ◽  
Chitin Binding Domain ◽  
Domain Fusion ◽  
Chitosan Films

scholarly journals Cellulose as an inert matrix for presenting cytokines to target cells: production and properties of a stem cell factor‒cellulose-binding domain fusion protein

1999 ◽  
Vol 339 (2) ◽  
pp. 429 ◽  
Author(s):  
J. Greg DOHENY ◽  
Eric J. JERVIS ◽  
M. Marta GUARNA ◽  
R. Keith HUMPHRIES ◽  
R. Antony J. WARREN ◽  
...  
Keyword(s):  
Stem Cell ◽  
Fusion Protein ◽  
Stem Cell Factor ◽  
Binding Domain ◽  
Target Cells ◽  
Cellulose Binding Domain ◽  
Inert Matrix ◽  
Domain Fusion ◽  
Cellulose Binding

scholarly journals Accelerated CO2 Hydration with Thermostable Sulfurihydrogenibium azorense Carbonic Anhydrase-Chitin Binding Domain Fusion Protein Immobilised on Chitin Support

2019 ◽  
Vol 20 (6) ◽  
pp. 1494 ◽  
Author(s):  
Juan Hou ◽  
Xingkang Li ◽  
Michal Kaczmarek ◽  
Pengyu Chen ◽  
Kai Li ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Fusion Protein ◽  
Large Scale ◽  
Economic Benefits ◽  
Binding Domain ◽  
Fusion Partner ◽  
Carbonic Anhydrases ◽  
Negative Effects ◽  
Chitin Binding Domain ◽  
Fusion Enzyme

Carbonic anhydrases (CAs) represent a group of enzymes that catalyse important reactions of carbon dioxide hydration and dehydration, a reaction crucial to many biological processes and environmental biotechnology. In this study we successfully constructed a thermostable fusion enzyme composed of the Sulfurihydrogenibium azorense carbonic anhydrase (Saz_CA), the fastest CA discovered to date, and the chitin binding domain (ChBD) of chitinase from Bacillus circulans. Introduction of ChBD to the Saz_CA had no major impact on the effect of ions or inhibitors on the enzymatic activity. The fusion protein exhibited no negative effects up to 60 °C, whilst the fusion partner appears to protect the enzyme from negative effects of magnesium. The prepared biocatalyst appears to be thermally activated at 60 °C and could be partially purified with heat treatment. Immobilisation attempts on different kinds of chitin-based support results have shown that the fusion enzyme preferentially binds to a cheap, untreated chitin with a large crystallinity index over more processed forms of chitin. It suggests significant potential economic benefits for large-scale deployment of immobilised CA technologies such as CO2 utilisation or mineralisation.

A streptavidin-cellulose-binding domain fusion protein that binds biotinylated proteins to cellulose

1994 ◽  
Vol 16 (6) ◽  
pp. 496-500 ◽  
Author(s):  
Khai D. Le ◽  
Neil R. Gilkes ◽  
Douglas G. Kilburn ◽  
Robert C. Miller ◽  
John N. Saddler ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Domain Fusion ◽  
Cellulose Binding

Crystallization of an intact GST-estrogen receptor hormone binding domain fusion protein

1998 ◽  
Vol 54 (3) ◽  
pp. 423-426 ◽  
Author(s):  
John M. Lally ◽  
Richard H. Newman ◽  
Philip P. Knowles ◽  
Suhail Islam ◽  
Arnold I. Coffer ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Fusion Protein ◽  
Binding Domain ◽  
Thin Plates ◽  
Hormone Binding ◽  
X Ray Diffraction ◽  
Visible Image ◽  
Domain Fusion ◽  
Hormone Binding Domain ◽  
Gst Fusion Proteins

Crystals of an intact GST–estrogen receptor hormone binding domain fusion protein have been grown from solutions of MPD. The crystals grew as clusters of thin plates and needles of maximum dimensions 100 × 20 × 1 µm but were unsuitable for X-ray diffraction analysis. However, examination by electron microscopy shows an ordered lattice in which the protein molecules are clearly visible. Image analysis of electron micrographs of the protein crystals revealed electron stain-excluding density which showed a two-domain trimeric structure in projection, with each molecule of dimensions 12.0 × 5.0 nm diameter. The use of GST-fusion proteins in crystallization are discussed.

scholarly journals Efficient siRNA delivery into primary cells by a peptide transduction domain–dsRNA binding domain fusion protein

2009 ◽  
Vol 27 (6) ◽  
pp. 567-571 ◽  
Author(s):  
Akiko Eguchi ◽  
Bryan R Meade ◽  
Yung-Chi Chang ◽  
Craig T Fredrickson ◽  
Karl Willert ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Sirna Delivery ◽  
Binding Domain ◽  
Primary Cells ◽  
Domain Fusion ◽  
Dsrna Binding ◽  
Peptide Transduction
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