Facile quantitative comparison of specific activities of fusion-tagged enzyme/mutants in cell lysates via prediction of their maximum adsorption by anti-tag antibody immobilized in microplate wells
Author:
Affiliation:
1. Unit for Analytical Probes and Protein Biotechnology
2. Key Laboratory of Clinical Laboratory Diagnostics of the Education Ministry
3. College of Laboratory Medicine
4. Chongqing Medical University
5. Chongqing 400016, China
Abstract
Maximum activities of 6His-tagged enzyme/mutants from lysates adsorbed on immobilized anti-tag antibody were predicted as specific activities for comparison.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2014/RA/C4RA03189J
Reference18 articles.
1. Advances in laboratory evolution of enzymes
2. Directed evolution drives the next generation of biocatalysts
3. Biocatalysts by evolution
4. High-throughput screening of enzyme libraries
5. In vitro enzyme evolution: the screening challenge of isolating the one in a million
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1. High-throughput estimation of specific activities of enzyme/mutants in cell lysates through immunoturbidimetric assay of proteins;Analytical Biochemistry;2017-10
2. Polyclonal Antibodies in Microplates to Predict the Maximum Adsorption Activities of Enzyme/Mutants from Cell Lysates;The Protein Journal;2017-04-19
3. Facile Alkaline Lysis of Escherichia coli Cells in High-Throughput Mode for Screening Enzyme Mutants: Arylsulfatase as an Example;Applied Biochemistry and Biotechnology;2016-02-22
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