Research Topics
| Hirokazu KouguchiSummaryAffiliation: Hokkaido Institute of Public Health Country: Japan Publications
| Collaborators
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Detail Information
Publications
Characterization of various recombinant antigens from Echinococcus multilocularis for use in the immunodiagnosisHirokazu Kouguchi
Hokkaido Institute of Public Health, Kita ku, Sapporo 060 0819, Japan
Protein J 24:57-64. 2005..In addition, the specific antibodies against #7 and #8s reacted with specific antigens in crude extract of E. multilocularis cyst, indicating that these antigens retained antigenicity common to native EmII/3 and AFFP, respectively...
Echinococcus multilocularis: two-dimensional Western blotting method for the identification and expression analysis of immunogenic proteins in infected dogsHirokazu Kouguchi
Hokkaido Institute of Public Health, N19 W12, Kita ku, Sapporo 060 0819, Japan
Exp Parasitol 124:238-43. 2010..Furthermore, recombinant hsp20 showed specific reactivity to the sera from infected dogs, suggesting that this molecule may facilitate the development of a practical vaccine...
Echinococcus multilocularis: purification and characterization of glycoprotein antigens with serodiagnostic potential for canine infectionHirokazu Kouguchi
Hokkaido Institute of Public Health, N19 W12, Kita ku, Sapporo, Japan
Exp Parasitol 128:50-6. 2011....
Characterization of emY162 encoding an immunogenic protein cloned from an adult worm-specific cDNA library of Echinococcus multilocularisYoshinobu Katoh
Department of Biological Science, Center for Infectious Disease Prevention, Hokkaido Institute of Public Health, Sapporo, Hokkaido 060 0819, Japan
Biochim Biophys Acta 1780:1-6. 2008..Immune responses to the recombinant EMY162 were studied by using serum from dogs infected with E. multilocularis. Strong IgG immune responses were detected in Western blots...
Identification of genetic loci affecting the establishment and development of Echinococcus multilocularis larvae in miceRyo Nakao
Department of Collaboration and Education, Research Center for Zoonosis Control, Hokkaido University, Kita 20, Nishi 10, Kita ku, Sapporo, Hokkaido 001 0020, Japan
Int J Parasitol 41:1121-8. 2011....
Early and presymptomatic detection of Wilson's disease at the mandatory 3-year-old medical health care examination in Hokkaido Prefecture with the use of a novel automated urinary ceruloplasmin assayKenji Nakayama
Hokkaido Institute of Public Health, North 19 West 12, Kita ku, Sapporo 060 0819, Hokkaido, Japan
Mol Genet Metab 94:363-7. 2008....
The vaccination potential of EMY162 antigen against Echinococcus multilocularis infectionHirokazu Kouguchi
Hokkaido Institute of Public Health, N19, W12, Kita ku, Sapporo 060 0819, Japan
Biochem Biophys Res Commun 363:915-20. 2007..These results may help in the development of a practical vaccine to reduce the level of alveolar echinococcosis in humans...
Quantitative detection of gene expression and toxin complex produced by Clostridium botulinum serotype D strain 4947Hirokazu Kouguchi
Hokkaido Institute of Public Health, N19, W12, Kita-ku, Sapporo 060-0819, Japan
J Microbiol Methods 67:416-23. 2006..Western blot analysis demonstrated that TC species in cell lysate were initially observed in the mid-exponential phase, while extracellular TCs were detected subsequently in the early stationary phase...
Characterization of the interaction between subunits of the botulinum toxin complex produced by serotype D through tryptic susceptibility of the isolated components and complex formsTomonori Suzuki
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri 099-2493, Japan
Microbiology 151:1475-83. 2005....
Characterization of toxin complex produced by a unique strain of Clostridium botulinum serotype D 4947Kimiko Hasegawa
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, Abashiri 099-2493, Japan
Protein J 23:371-8. 2004..We have established a new method to separate the unique D-4947 NT from the complex, which will yield valuable information on structure of botulinum toxin...
Complete subunit structure of the Clostridium botulinum type D toxin complex via intermediate assembly with nontoxic componentsShingo Mutoh
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri 099-2493, Japan
Biochemistry 42:10991-7. 2003..In conclusion, the complete subunit composition of mature L-TC is deduced to be a dodecamer assembled by a single NT, a single NTNHA, two HA-70, four HA-33, and four HA-17 molecules...
Spontaneous nicking in the nontoxic-nonhemagglutinin component of the Clostridium botulinum toxin complexYoshimasa Sagane
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri 099-2493, Japan
Biochem Biophys Res Commun 292:434-40. 2002....
In vitro reconstitution of the Clostridium botulinum type D progenitor toxinHirokazu Kouguchi
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri 099-2493, Japan
J Biol Chem 277:2650-6. 2002..We conclude that the M toxin forms first by assembly of NT with NTNHA and is subsequently converted to the L toxin by assembly with HA-70 and HA-33/17...
