| dc.contributor.author |
Mazitsos, CF |
en |
| dc.contributor.author |
Rigden, DJ |
en |
| dc.contributor.author |
Tsoungas, PG |
en |
| dc.contributor.author |
Clonis, YD |
en |
| dc.date.accessioned |
2014-06-06T06:45:12Z |
|
| dc.date.available |
2014-06-06T06:45:12Z |
|
| dc.date.issued |
2002 |
en |
| dc.identifier.issn |
00142956 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1046/j.1432-1033.2002.03211.x |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/2296 |
|
| dc.subject |
Affinity chromatography |
en |
| dc.subject |
Biomimetic ligands |
en |
| dc.subject |
Galactose dehydrogenase |
en |
| dc.subject |
Molecular modelling |
en |
| dc.subject |
Triazine dyes |
en |
| dc.subject.other |
carbohydrate derivative |
en |
| dc.subject.other |
dye |
en |
| dc.subject.other |
galactose dehydrogenase |
en |
| dc.subject.other |
ligand |
en |
| dc.subject.other |
affinity chromatography |
en |
| dc.subject.other |
affinity labeling |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
biomimetics |
en |
| dc.subject.other |
chemical structure |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme binding |
en |
| dc.subject.other |
enzyme immobilization |
en |
| dc.subject.other |
enzyme inactivation |
en |
| dc.subject.other |
enzyme purification |
en |
| dc.subject.other |
molecular model |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein function |
en |
| dc.subject.other |
Pseudomonas fluorescens |
en |
| dc.subject.other |
Amino Acid Sequence |
en |
| dc.subject.other |
Chromatography, Affinity |
en |
| dc.subject.other |
Coloring Agents |
en |
| dc.subject.other |
Galactose Dehydrogenases |
en |
| dc.subject.other |
Hydrogen Bonding |
en |
| dc.subject.other |
Imidazoles |
en |
| dc.subject.other |
Ligands |
en |
| dc.subject.other |
Models, Chemical |
en |
| dc.subject.other |
Models, Molecular |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Oxidoreductases |
en |
| dc.subject.other |
Protein Binding |
en |
| dc.subject.other |
Protein Conformation |
en |
| dc.subject.other |
Protein Structure, Tertiary |
en |
| dc.subject.other |
Pseudomonas fluorescens |
en |
| dc.subject.other |
Sepharose |
en |
| dc.subject.other |
Sequence Homology, Amino Acid |
en |
| dc.subject.other |
Spectrophotometry |
en |
| dc.subject.other |
Sulfhydryl Reagents |
en |
| dc.subject.other |
Bacteria (microorganisms) |
en |
| dc.subject.other |
Negibacteria |
en |
| dc.subject.other |
Pseudomonas |
en |
| dc.subject.other |
Pseudomonas fluorescens |
en |
| dc.title |
Galactosyl-mimodye ligands for Pseudomonas fluorescens β-galactose dehydrogenase: Design, synthesis and evaluation |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1046/j.1432-1033.2002.03211.x |
en |
| heal.publicationDate |
2002 |
en |
| heal.abstract |
Protein molecular modelling and ligand docking were employed for the design of anthraquinone galactosyl-biomimetic dye ligands (galactosylmimodyes) for the target enzyme galactose dehydrogenase (GaDH). Using appropriate modelling methodology, a GaDH model was build based on a glucose-fructose oxidoreductase (GFO) protein template. Subsequent computational analysis predicted chimaeric mimodye-ligands comprising a NAD-pseudomimetic moiety (anthraquinone diaminobenzosulfonic acid) and a galactosyl-mimetic moiety (2-amino-2-deoxygalactose or shikimic acid) bearing an aliphatic 'linker' molecule. In addition, the designed mimodye ligands had an appropriate in length and chemical nature 'spacer' molecule via which they can be attached onto a chromatographic support without steric clashes upon interaction with GaDH. Following their synthesis, purification and analysis, the ligands were immobilized to agarose. The respective affinity adsorbents, compared to other conventional adsorbents, were shown to be superior affinity chromatography materials for the target enzyme, Pseudomonas fluorescens β-galactose dehydrogenase. In addition, these mimodye affinity adsorbents displayed good selectivity, binding low amounts of enzymes other than GaDH. Further immobilized dye-ligands, comprising different linker and/or spacer molecules, or not having a biomimetic moiety, had inferior chromatographic behavior. Therefore, these new mimodyes suggested by computational analysis, are candidates for application in affinity labeling and structural studies as well as for purification of galactose dehydrogenase. |
en |
| heal.journalName |
European Journal of Biochemistry |
en |
| dc.identifier.issue |
22 |
en |
| dc.identifier.volume |
269 |
en |
| dc.identifier.doi |
10.1046/j.1432-1033.2002.03211.x |
en |
| dc.identifier.spage |
5391 |
en |
| dc.identifier.epage |
5405 |
en |