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Start Over Author "Deng, G. Y." Journal bioconjugate chemistry
2 results on '"Deng, G. Y."'

1. On−Off Switching of Enzymatic Reaction by Recombinant Calmodulin on a Solid-Phase Matrix

Author

Kobatake, E., Mitomo, K., Haruyama, T., Aizawa, M., Deng, G. Y., and Kato, S.

Abstract

A fusion protein consisting of human calmodulin (CaM) and glutathione S-transferase (GST) was produced by gene fusion. The fusion protein was overexpressed in Escherichia coli as a soluble form and purified with one-step affinity chromatography using glutathione−Sepharose. The protein had the modulating activity of CaM and the binding capability to glutathione of GST. Phosphodiesterase, which is a CaM dependent enzyme, was activated by the fusion protein, with the Ca2+ level equal to the level equivalent to a native CaM. Furthermore, CaM could be immobilized on a solid-phase matrix through the use of GST moiety while its modulating activity was retained. Phosphodiesterase activity was switched on and off by the immobilized CaM with or without Ca2+, and repeated use of CaM was demonstrated.

Published
1996

2. On-off switching of enzymatic reaction by recombinant calmodulin on a solid-phase matrix.

Author

Kobatake E, Mitomo K, Haruyama T, Aizawa M, Deng GY, and Kato S

Subjects
3',5'-Cyclic-AMP Phosphodiesterases metabolism, Amino Acid Sequence, Base Sequence, Calcium pharmacology, Calmodulin biosynthesis, Calmodulin isolation & purification, Cloning, Molecular, DNA Primers, Enzyme Activation, Enzymes, Immobilized metabolism, Escherichia coli, Glutathione metabolism, Glutathione Transferase biosynthesis, Glutathione Transferase isolation & purification, Humans, Molecular Sequence Data, Plasmids, Polymerase Chain Reaction, Recombinant Fusion Proteins biosynthesis, Recombinant Fusion Proteins isolation & purification, Calmodulin metabolism, Glutathione Transferase metabolism, Recombinant Fusion Proteins metabolism
Abstract

A fusion protein consisting of human calmodulin (CaM) and glutathione S-transferase (GST) was produced by gene fusion. The fusion protein was overexpressed in Escherichia coli as a soluble form and purified with one-step affinity chromatography using glutathione-Sepharose. The protein had the modulating activity of CaM and the binding capability to glutathione of GST. Phosphodiesterase, which is a CaM dependent enzyme, was activated by the fusion protein, with the Ca2+ level equal to the level equivalent to a native CaM. Furthermore, CaM could be immobilized on a solid-phase matrix through the use of GST moiety while its modulating activity was retained. Phosphodiesterase activity was switched on and off by the immobilized CaM with or without Ca2+, and repeated use of CaM was demonstrated.

Published
1996
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