T. Teshima

Preparation of Thermus thermophilus holo-chaperonin-immobilized microspheres with high ability to facilitate protein refolding.

H. Taguchi, A. Kondo, H. Fukuda, 2000, Biotechnology and bioengineering.

Operation conditions of enzyme refolding by chaperonin and recycle system using ultrafiltration

Y. Ishii, A. Kondo, H. Fukuda, 1997 .

Preparation of immobilized enzyme with high activity using affinity tag based on proteins A and G

A. Kondo, T. Teshima, 1995, Biotechnology and bioengineering.

Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES

A. Kondo, H. Fukuda, T. Teshima, 1997, Applied Microbiology and Biotechnology.

Development of Efficient Protein Refolding Systems Using Chaperonins

A. Kondo, H. Fukuda, J. Kohda, 2000 .

Affinity Purification of Fusion Chaperonin Cpn60‐(His)6 from Thermophilic Bacterium BacillusStrain MS and Its Use in Facilitating Protein Refolding and Preventing Heat Denaturation

A. Kondo, H. Fukuda, M. Yohda, 2000, Biotechnology progress.

Protein refolding system using holo-chaperonin from the thermophilic bacterium Thermus thermophilus

H. Taguchi, A. Kondo, H. Fukuda, 1998 .

Affinity Purification and Immobilization of Fusion Chaperonin GroEL-(His)6 and Its Utilization to Mediate Protein Refolding

A. Kondo, H. Fukuda, T. Teshima, 1998 .