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Dive into the research topics where Yuki Hamada is active.

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Featured researches published by Yuki Hamada.


Allergy | 2006

Comparison of allergenicity and allergens between fish white and dark muscles

A. Kobayashi; Hiroyuki Tanaka; Yuki Hamada; Shoichiro Ishizaki; Yuji Nagashima; Kazuo Shiomi

Background:  Fish is one of the most frequent causes of immunoglobulin E (IgE)‐mediated food allergy. Although the fish dark muscle is often ingested with the white muscle, no information about its allergenicity and allergens is available.


Food and Chemical Toxicology | 2003

Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels.

Yuki Hamada; H. Tanaka; Shoichiro Ishizaki; Masami Ishida; Yuji Nagashima; Kazuo Shiomi

Three species of mackerels (Scomber japonicus, S. australasicus and S. scombrus) are widely consumed and considered to be most frequently involved in incidents of IgE-mediated fish allergy in Japan. In this study, parvalbumin, a possible candidate for the major allergen, was purified from the white muscle of three species of mackerels by gel filtration on Sephadex G-75 and reverse-phase HPLC on TSKgel ODS-120T. All the purified preparations from three species gave a single band of about 11 kDa and were clearly identified as parvalbumins by analyses of their partial amino acid sequences. In ELISA experiments, four of five sera from fish-allergic patients reacted to all the purified parvalbumins, demonstrating that parvalbumin is the major allergen in common with the mackerels. Antigenic cross-reactivity among the mackerel parvalbumins was also established by ELISA inhibition experiments. A cDNA library was constructed from the white muscle of S. japonicus and the cDNA encoding parvalbumin was cloned. The amino acid sequence translated from the nucleotide sequence revealed that the S. japonicus parvalbumin is composed of 108 residues, being a member of beta-type parvalbumins.


Physical Review Letters | 2013

Higgs amplitude mode in the BCS superconductors Nb1-xTi(x)N induced by terahertz pulse excitation.

Ryusuke Matsunaga; Yuki Hamada; Kazumasa Makise; Yoshinori Uzawa; Hirotaka Terai; Zhen Wang; Ryo Shimano

Ultrafast responses of BCS superconductor Nb(1-x)Ti(x)N films in a nonadiabatic excitation regime were investigated by using terahertz (THz) pump-THz probe spectroscopy. After an instantaneous excitation with the monocycle THz pump pulse, a transient oscillation emerges in the electromagnetic response in the BCS gap energy region. The oscillation frequency coincides with the asymptotic value of the BCS gap energy, indicating the appearance of the theoretically anticipated collective amplitude mode of the order parameter, namely the Higgs amplitude mode. Our result opens a new pathway to the ultrafast manipulation of the superconducting order parameter by optical means.


Toxicon | 1999

Subcellular distribution of tetrodotoxin in puffer fish liver

Yuji Nagashima; Yuki Hamada; Hideki Ushio; Sachio Nishio; Kuniyoshi Shimakura; Kazuo Shiomi

The liver homogenate of puffer fish was fractionated into blood cell, nuclear, mitochondrial, microsomal and cytosol fractions by the differential centrifugation method. All the five fractions were toxic to mice, although the toxin amount was significantly high in the cytosol fraction. Analyses by HPLC and LC-FABMS demonstrated that tetrodotoxin is the major toxic principle in each fraction. These results reveal that tetrodotoxin is widely distributed in organelles in liver cells, though predominantly in the cytosol fraction.


Fisheries Science | 2007

Characteristics of burnt meat in cultured yellowtail Seriola quinqueradiata

Daisy Arroyo Mora; Yuki Hamada; Akira Okamoto; Ayumi Tateishi; Katsuyasu Tachibana

In order to understand the characteristics of burnt meat in cultured yellowtail Seriola quinqueradiata, fish were kept at two different temperatures (13 and 30°C) and slaughtered by either spinal cord destruction (SCD) or suffocation in air (SA). Early postmortem changes during storage at 32°C were analyzed by rheological, biochemical, and histological methods. The burnt meat (with lightness parameter, L*≥55) was observed at 1-h storage in the SA 30°C group, at 2 h in SCD 30°C, and at 4 h in SA 13°C; meat was normal for the SCD 13°C group until 6h of storage. Breaking strength scores were higher for the normal meat (200 g/cm2) than burnt meat (70 g/cm2) at 4 h of storage. Expressible water content was higher for the burnt meat than for the normal meat. Adenosine triphosphate concentrations for the SCD groups were higher than for the SA counterparts. Moreover, pH decrease was much faster in the 30°C groups, showing pH 5.6 at 2 h of storage. A negative correlation between the pH and lactic acid contents in muscle (P<0.001) was found. Histological analysis evidenced a larger pericellular area (40%) in the burnt samples than in the normal samples (16%). It was confirmed that a higher fish-keeping water temperature and a stressful slaughter method (faster glycolytic process) were determinative factors that influence the occurrence of burnt muscle in yellowtail, and that the effect of the former is larger than the latter.


Food Additives and Contaminants Part A-chemistry Analysis Control Exposure & Risk Assessment | 2007

Allergenicity and allergens of amphipods found in nori (dried laver)

Kanna Motoyama; Yuki Hamada; Yuji Nagashima; Kazuo Shiomi

Gammaridean and caprellid amphipods, crustaceans of the order Amphipoda, inhabit laver culture platforms and, hence, are occasionally found in nori (dried laver) sheets. Amphipods mixed in nori may cause allergic reactions in sensitized patients, as is the case with other crustaceans, such as shrimp and crab, members of the order Decapoda. In this study, dried samples of amphipods (unidentified) found in nori and fresh samples of gammaridean amphipod (Gammarus sp., not accurately identified) and caprellid amphipod (Caprella equilibra) were examined for allergenicity and allergens using two species of decapods (black tiger prawn and spiny lobster) as references. When analyzed by ELISA, sera from crustacean-allergic patients reacted to extracts from amphipod samples, although less potently than to the extracts from decapods. In IgE-immunoblotting, a 37-kDa protein was found to be the major allergen in amphipods. Based on the molecular mass and the cross-reactivity with decapod tropomyosin evidenced by inhibition ELISA and inhibition immunoblotting, the 37-kDa protein was identified as amphipod tropomyosin.


Genome Announcements | 2014

Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM 18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic Organisms

Toshiaki Kudo; Akihiro Kidera; Muneaki Kida; Ayumi Kawauchi; Ryo Shimizu; Tomomi Nakahara; Xiaochi Zhang; Akinori Yamada; Masao Amano; Yuki Hamada; Shigeto Taniyama; Osamu Arakawa; Asami Yoshida; Kenshiro Oshima; Wataru Suda; Hirokazu Kuwahara; Yuichi Nogi; Keiko Kitamura; Masahiro Yuki; Toshiya Iida; Shigeharu Moriya; Tetsushi Inoue; Yuichi Hongoh; Masahira Hattori; Moriya Ohkuma

ABSTRACT Four Psychrobacter strains, JCM 18900, JCM 18901, JCM 18902, and JCM 18903, related to either Psychrobacter nivimaris or Psychrobacter cibarius, were isolated from frozen marine animals. The genome information of these four strains will be useful for studies of their physiology and adaptation properties to frozen conditions.


Bioscience, Biotechnology, and Biochemistry | 2001

Identification of collagen as a new fish allergen.

Yuki Hamada; Yuji Nagashima; Kazuo Shiomi


Food Chemistry | 2005

Allergenicity of crustacean extractives and its reduction by protease digestion

Kuniyoshi Shimakura; Yumiko Tonomura; Yuki Hamada; Yuji Nagashima; Kazuo Shiomi


Fisheries Science | 1999

Two Classes of Allergens, Parvalbumins and Higher Molecular Weight Substances, in Japanese Eel and Bigeye Tuna.

Kazuo Shiomi; Yuki Hamada; Kaori Sekiguchi; Kuniyoshi Shimakura; Yuji Nagashima

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Kazuo Shiomi

Tokyo University of Marine Science and Technology

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Yuji Nagashima

Tokyo University of Marine Science and Technology

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Akira Okamoto

Tokyo University of Marine Science and Technology

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Hirotaka Terai

National Institute of Information and Communications Technology

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Kazumasa Makise

National Institute of Information and Communications Technology

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Zhen Wang

Chinese Academy of Sciences

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