Use of a novel affinity tag selected with a bacterial random peptide library for improving activity retention of glutathione S-transferase adsorbed on a polystyrene surface-Reference-Cited by-同舟云学术

Use of a novel affinity tag selected with a bacterial random peptide library for improving activity retention of glutathione S-transferase adsorbed on a polystyrene surface

Published:2004-06 Issue:4-6 Volume:28 Page:207-214
ISSN:1381-1177
Container-title:Journal of Molecular Catalysis B: Enzymatic
language:en
Short-container-title:Journal of Molecular Catalysis B: Enzymatic

Author:

Sakiyama Takaharu,Ueno Shunsuke,Imamura Koreyoshi,Nakanishi Kazuhiro

Publisher

Elsevier BV

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Reference25 articles.

1. The immunochemistry of sandwich elisas—VI. Greater than 90% of monoclonal and 75% of polyclonal anti-fluorescyl capture antibodies (CAbs) are denatured by passive adsorption

2. Use of monoclonal antibodies to detect conformational alterations in lactate dehydrogenase isoenzyme 5 on heat denaturation and on adsorption to polystyrene plates

3. Adsorption of the protein antigen myoglobin affects the binding of conformation-specific monoclonal antibodies

4. Oriented immobilization of proteins

5. Improving the activity of immobilized subtilisin by site-directed attachment through a genetically engineered affinity tag

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