Characterization of Gly-d-Phe, Gly-l-Leu, and d-Phe as affinity ligands to thermolysin
Author:
Publisher
Elsevier BV
Subject
Biotechnology
Reference28 articles.
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Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Effects of Site-Directed Mutagenesis of the Loop Residue of the N-Terminal Domain Gly117 of Thermolysin on Its Catalytic Activity;Bioscience, Biotechnology, and Biochemistry;2010-12-23
2. Insights into the Catalytic Roles of the Polypeptide Regions in the Active Site of Thermolysin and Generation of the Thermolysin Variants with High Activity and Stability;Journal of Biochemistry;2008-10-25
3. Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2008-03
4. Improving the activity and stability of thermolysin by site-directed mutagenesis;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2007-10
5. Improvement in Performance of Affinity Gels Containing Gly-D-Phe as a Ligand to Thermolysin Due to Increasing the Spacer Chain Length;Bioscience, Biotechnology, and Biochemistry;2007-08-23
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