Research Topics
| Teruaki ShirozaSummaryAffiliation: Nihon University Country: Japan Publications
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Detail Information
Publications
Sequence analysis of two ScFv genes of MAbs against Streptococcus mutans glucosyltransferaseKimi Matsumoto
Department of Biochemistry and Molecular Biology, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba, Japan
Hybridoma (Larchmt) 24:175-81. 2005....
Construction of a chimeric shuttle plasmid via a heterodimer system: secretion of an scFv protein from Bacillus brevis cells capable of inhibiting hemagglutinationT Shiroza
Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Chiba, Japan
Biosci Biotechnol Biochem 65:389-95. 2001..The chimeric shuttle plasmid was readily constructed by simple re-circularization and a B. brevis transformant producing the scFv protein in the culture fluid was isolated...
Production of a single-chain variable fraction capable of inhibiting the Streptococcus mutans glucosyltransferase in Bacillus brevis: construction of a chimeric shuttle plasmid secreting its gene productTeruaki Shiroza
Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Matsudo, 271 8587, Chiba, Japan
Biochim Biophys Acta 1626:57-64. 2003..brevis transformant following the construction of a chimeric shuttle plasmid, which was accomplished by employing a new heterodimer system...
Production of functional ScFv inhibiting Streptococcus mutans glucosyltransferase activity from a hybridoma P126Hiroyoshi Tagawa
Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Chiba, Japan
Hybrid Hybridomics 23:305-10. 2004..The purified ScFv antibody recognized the recombinant (r) GTF-I proteins and was capable of inhibiting the WIG synthesis of rGTF-I...
Expression of the gtfI gene from Streptococcus sobrinus in Streptococcus anginosus using integration-mediated transformation systemNoriko Shinozaki-Kuwahara
Department of Microbiology, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba 271 8587, Japan
Biochim Biophys Acta 1722:189-99. 2005..anginosus. These observations strongly suggest that the construction of S. anginosus integrant expressing S. sobrinus gtfI gene using this transformation system may be an effective means of analysis of cariogenic biofilm formation...
Functional analysis of the thioredoxin domain in Porphyromonas gingivalis HBP35Teruaki Shiroza
Department of Chemistry, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba, Japan
Biosci Biotechnol Biochem 72:1826-35. 2008..Transformant harboring the native hbp35 could complement the dsbA mutation, suggesting a role of disulfide bond formation of this protein in P. gingivalis cells. Possible roles of the Cys residues in complementation are discussed...
Further development of an electroosmotic medium pump system for preparative disk gel electrophoresisMitsuo Hayakawa
Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba 271 8587, Japan
Anal Biochem 313:60-7. 2003..5% T native-PAGE and subsequential sodium dodecyl sulfate-PAGE system. This device enhances the possibility of continuous electrophoretic fractionation of complex protein mixtures on a preparative scale...
Proteomics-based analysis of a counter-oxidative stress system in Porphyromonas gingivalisSoichiro Okano
Department of Biochemistry and Molecular Biology, Nihon University School of Dentistry at Matsudo, 2-870-1 Sakaecho-Nishi, Matsudo, Chiba 271-8587 Chiba, Japan
Proteomics 6:251-8. 2006..Oxidative stress was found to affect the expression of numerous proteins in P. gingivalis cells. In particular, the levels of HtpG, GroEL, DnaK, AhpC, TPR domain protein, and trigger factor were substantially increased...
A 35-kDa co-aggregation factor is a hemin binding protein in Porphyromonas gingivalisYasuko Shibata
Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Chiba 271 8587, Japan
Biochem Biophys Res Commun 300:351-6. 2003..These results demonstrated that 35-kDa protein is one of the hemin binding proteins in P. gingivalis and suggested that hemin binding ability of 35-kDa protein is important for the expression of virulence in P. gingivalis...
Cloning and nucleotide sequence analysis of the Streptococcus sobrinus gtfU gene that produces a highly branched water-soluble glucanNobuhiro Hanada
Department of Oral Science, National Institute of Infectious Diseases, 1 23 1 Toyama, Sinjuku ku, Tokyo 162 8640, Japan
Biochim Biophys Acta 1570:75-9. 2002..coli MD66 clone was similar to S. sobrinus GTF-S1. Biological properties and a linkage analysis of the glucans by 13C NMR spectrometry revealed that the protein produced by the E. coli MD66 clone was GTF-S1...
