Ken-Ji Yokoi
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Research Interests
Ken-Ji Yokoi has a total of 19 co-authors. Here are the top co-authors by number of shared publications:
Akira Taketo
6 shared publications- Ken-Ichi Kodaira
B Molecular Biology Group, Faculty of Engineering , Toyama University , Toyama , Japan
5 shared publications Ayanori Yamakawa
4 shared publications- Kei-Ichi Shozen
Agriculture, Forestry and Fisheries Department, Toyama Prefecture Government, Toyama, Japan
2 shared publications Mitsuru Kondo
2 shared publicationsShinya Kuzuwa
2 shared publications
Latest Publications
- 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).