Ken-Ichi Kodaira
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Ken-Ichi Kodaira has a total of 18 co-authors. Here are the top co-authors by number of shared publications:
Akira Taketo
E Department of Applied Physics and Chemistry , Fukui University of Technology , Fukui , Japan
6 shared publications- Ken-Ji Yokoi
Toyama Prefectural Food Research Institute, 360 Yoshioka, Toyama 939-8153, Japan
5 shared publications Ayanori Yamakawa
D Biochemistry Division, Department of Material Science , Wakayama National College of Technology , Wakayama , Japan
4 shared publicationsShinya Kuzuwa
B Molecular Biology Group, Faculty of Engineering , Toyama University , Toyama , Japan
2 shared publicationsAkinori Iguchi
1 shared publicationGo Nishitani
1 shared publication
Latest Publications
- Open Access
- 2 June 2016
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 80 (6) , 1238-1242
Aureolysin of Staphylococcus warneri M accelerates its proteolytic cascade, and participates in biofilm formation
The aureolysin (Aur) gene of S. warneri M (aurWM) was cloned and sequenced. Analyses of the aurWM-inactivated mutant (S. warneri Mau) suggested that AurWM was probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease), whereas considerable amount of mature-PROC protease (homolog of SspB cysteine protease) accumulated without AurWM. Additionally, AurWM appeared to affect biofilm formation in an uncertain suppressive way.
- 2 June 2016
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 80 (6) , 1238-1242
Open AccessAureolysin of Staphylococcus warneri M accelerates its proteolytic cascade, and participates in biofilm formation
The aureolysin (Aur) gene of S. warneri M (aurWM) was cloned and sequenced. Analyses of the aurWM-inactivated mutant (S. warneri Mau) suggested that AurWM was probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease), whereas considerable amount of mature-PROC protease (homolog of SspB cysteine protease) accumulated without AurWM. Additionally, AurWM appeared to affect biofilm formation in an uncertain suppressive way.
- 1 January 2011
- Published by Springer Nature
- p. 867-872
Microvirus
- 1 June 2002
- Published by Taylor & Francis in The Journal of Biochemistry, Molecular Biology and Biophysics
- Vol. 6 (3) , 185-191
Characterization of the Major Tail Protein gpP Encoded by Lactobacillus plantarum Phage ϕ gle
Lactobacillus plantarum temperate phage phi g1e encodes a major virion protein gpP. In the present study, the gpP protein was overproduced in Escherichia coli under plac, and purified. Like the native-gpP protein from phi gle particles (Kakikawa et al., 1996), the purified-gpP protein had an apparent molecular mass of 26.0 kDa on SDS polyacrylamide gel electrophoresis (PAGE), larger than that (18.8 kDa) predicted from the DNA sequence, and was deficient in the first methionine as revealed by the N-terminal protein sequencing. In addition, analysis by immunoelectron microscopy demonstrated that immunogold particles (associated with antigpP-sera) specifically bound to the tails of phi gle particles, indicating that gpP is a main tail component (putatively a tube protein).
- 1 June 2002
- Published by Taylor & Francis in The Journal of Biochemistry, Molecular Biology and Biophysics
- Vol. 6 (3) , 185-191
Characterization of the Major Tail Protein gpP Encoded by Lactobacillus plantarum Phage ϕ gle
Lactobacillus plantarum temperate phage phi g1e encodes a major virion protein gpP. In the present study, the gpP protein was overproduced in Escherichia coli under plac, and purified. Like the native-gpP protein from phi gle particles (Kakikawa et al., 1996), the purified-gpP protein had an apparent molecular mass of 26.0 kDa on SDS polyacrylamide gel electrophoresis (PAGE), larger than that (18.8 kDa) predicted from the DNA sequence, and was deficient in the first methionine as revealed by the N-terminal protein sequencing. In addition, analysis by immunoelectron microscopy demonstrated that immunogold particles (associated with antigpP-sera) specifically bound to the tails of phi gle particles, indicating that gpP is a main tail component (putatively a tube protein).