Kagoshima Womens Junior College

Kagoshima-shi, Japan

Kagoshima Womens Junior College

Kagoshima-shi, Japan
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Zaqout M.S.K.,University of Occupational and Environmental Health Japan | Sumizawa T.,Kagoshima Womens Junior College | Igisu H.,Fukuoka Central Health Evaluation and Promotion Center | Wilson D.,University of Occupational and Environmental Health Japan | And 2 more authors.
Environmental Health and Preventive Medicine | Year: 2012

Objective Measurement of released lactate dehydrogenase (LDH) activity, a commonly used marker of lethal cell injury in both in vitro and in vivo screenings, has been used to assess the cytotoxicity of nanoparticles (NPs), chemical compounds, and environmental factors. We have recently demonstrated that titanium dioxide (TiO 2) particles bind to several serum proteins. In the present study we investigated the binding of TiO 2 NPs to LDH. Methods Purified LDH was incubated with TiO 2 NPs at 37°C for 1 h. The particles were then sedimented by centrifugation, and the activity and quantity of LDH in the supernatant and precipitated fraction were analyzed. Results Incubation with TiO 2 reduced the LDH activity in the supernatant in a dose-dependent manner, while LDH activity in the precipitated fraction increased in a dosedependent manner. Moreover, sodium dodecyl sulfatepolyacrylamide gel electrophoresis analysis revealed a TiO 2 dose-dependent reduction in the quantity of LDH protein in the supernatant and an increase of LDH in particulate re-suspensions. Conclusions These findings, although based on a purified form of LDH, suggest that TiO 2 NPs bind to LDH, and consequently, TiO 2 NP-induced toxicity could be underestimated by the LDH activity assay. © The Japanese Society for Hygiene 2011.

Ishiguro K.,Japan National Agricultural Research Center | Yoshinaga M.,Japan National Agricultural Research Center | Kai Y.,Japan National Agricultural Research Center | Maoka T.,Research Institute for Production Development | And 2 more authors.
Breeding Science | Year: 2010

The total carotenoid contents in eight sweetpotato (Ipomoea batatas L.) cultivars or breeding lines with yellow flesh were evaluated by absorption spectrophotometry and compared to those of four cultivars with orange flesh. The content ranged from 1.3 mg/100 g dry weight to 3.9 mg/100 g dry weight in yellow-fleshed cultivars and from 13.5 mg/100 g dry weight to 39.9 mg/100 g dry weight in orange-fleshed cultivars. Seventeen carotenoids were detected in yellow- and orange-fleshed sweetpotato by HPLC analysis. The amount of carotenoids analyzed by HPLC correlated highly with the carotenoid content analyzed spectrophotometrically. The main carotenoids were β-carotene 5,8;5′,8′-diepoxide (ca. 32%-51%) and β-cryptoxanthin 5,8-epoxide (ca. 11%-30%) in yellow-fleshed cultivars/lines, while β-carotene (ca. 80%-92%) was dominant in orange-fleshed cultivars. These results suggest that the content of each carotenoid differs according to flesh color, yellow or orange, although the carotenoid component in the yellow and orange flesh was almost identical. The antioxidative activities of carotenoids isolated from yellow-fleshed weetpotato were analyzed by the 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) radical-scavenging activity. The activity of ipomoeaxanthin A was comparable to β-carotene, and that of β-cryptoxanthin 5,8- epoxide was the lowest. The carotenoids in yellow-fleshed sweetpotato might contribute to the prevention of some diseases due to their antioxidative effect. β-carotene epoxides and β-crypthoxanthin epoxides, which are abundant in the yellow-fleshed cultivars, are noteworthy components for the breeding selection of sweetpotato with deep yellow flesh.

Okuno S.,Japan National Agriculture and Food Research Organization | Ishiguro K.,Japan National Agriculture and Food Research Organization | Ishiguro K.,Japan National Agricultural Research Center | Yoshinaga M.,Japan National Agriculture and Food Research Organization | And 2 more authors.
Japan Agricultural Research Quarterly | Year: 2010

In 2002, we reported that sweetpotato leaves contained six caffeic acid derivatives, namely, caffeic (CA), chlorogenic (5-O-caffeoylquinic acid, ChA), 3,4-di-O-caffeoylquinic (3,4-diCQA), 3,5-di-Ocaffeoylquinic (3,5-diCQA), 4,5-di-O-caffeoylquinic (4,5-diCQA), and 3,4,5-tri-O-caffeoylquinic (3,4,5-triCQA) acids, which are known to have many physiological functions. A new sweetpotato cultivar 'Suioh' was developed for use of its tops as an edible green by KONARC. It is important to analyze the caffeic acid derivatives efficiently with high-performance liquid chromatography (HPLC) in order to continue developing or selecting new cultivars with higher contents of these compounds in their tops. For this purpose, a short column (4.6 i.d. × 75 mm) packed with small ODS particles (3 μm) was used without replacing the conventional HPLC apparatus and the time for one analysis per sample was decreased to 26 min, from 90 min, which was the analysis time reported in 2002. With the new HPLC conditions, we could quantify the six caffeic acid derivatives in lyophilized leaf samples from 529 sweetpotato cultivars, which compose approximately one-third of the cultivars maintained at KONARC.

Matuda S.,National Institute of Fitness and Sports in Kanoya | Arimura T.,Tokyo Medical and Dental University | Kimura A.,Tokyo Medical and Dental University | Takekura H.,National Institute of Fitness and Sports in Kanoya | And 2 more authors.
Biochimica et Biophysica Acta - General Subjects | Year: 2010

Background: It is not known if the dihydrolipoamide succinyltransferase (DLST) gene, a mitochondrial protein, undergoes alternative splicing. We identified an uncharacterized protein reacting with an anti-DLST antibody in the I bands of myofibrils in rat skeletal muscle. Methods: Immunocytochemical staining with an anti-DLST antibody, the purification and amino acid sequence analysis of the protein, and the isolation and sequencing of the protein's cDNA were carried out to clarify the properties of the protein and its relationship to the DLST gene. Results: A pyrophosphate concentration >10 mM was necessary to extract the protein from myofibrils in the presence of salt with a higher concentration than 0.6 M, at an alkaline pH of 7.5-8.0. The protein corresponded to the amino acid sequence of the C-terminal side of DLST. The cDNAs for this protein were splicing variants of the DLST gene, with deletions of both exons 2 and 3, or only exon 2 or 3. These variants possessed an open reading frame from an initiation codon in exon 8 of the DLST gene to a termination codon in exon 15, generating a protein with a molecular weight of 30 kDa. Conclusions: The DLST gene undergoes alternative splicing, generating the protein isolated from the I bands of myofibrils. General significance: The DLST gene produces two different proteins with quite different functions via alternative splicing. © 2009.

Ujihara K.,Japan National Agricultural Research Center | Yoshimoto M.,Kagoshima Womens Junior College | Wada K.,The University of Okinawa | Takahashi M.,The University of Okinawa | Suda I.,Japan National Agricultural Research Center
Nippon Shokuhin Kagaku Kogaku Kaishi | Year: 2013

The effects of heating temperature and time on browning, DPPH-radical scavenging activity and polyphenollike activity of molasses from sugarcane were investigated. The browning, DPPH-radical scavenging activity and polyphenol-like activity of molasses heated to between 120°C and 160°C were increased in comparison with unheated molasses. The browning of molasses heated to 120°C and 140°C increased with heating time, and was nearly 9.5 times greater than unheated molasses after heating for 60 minutes. The browning of molasses heated to 160°C exponentially increased after heating for 10 minutes, and was nearly 16.7 times greater than unheated molasses after heating for 20 minutes. The DPPH-radical scavenging activity of molasses heated to 120°C for 50 minutes, 140°C for 10 minutes, and 160°C for 10 minutes was four times greater than that of unheated molasses. The alterations in DPPH-radical scavenging activity were similar to the polyphenol-like activity pattern with heat-processing. The heated molasses with the highest polyphenol-like activity, processed at 160°C for 20 minutes, showed stronger antimutagenicity than unheated molasses. These results indicate that the heat-processing of sugarcane molasses is a viable method for the enhancement of food functions in sugarcane molasses.

Yamanoue T.,Kagoshima University | Fouser R.J.,Seoul National University | Wada T.,National Institute of Fitness and Sports in Kanoya | Hidaka M.,Kagoshima University | And 17 more authors.
Proceedings ACM SIGUCCS User Services Conference | Year: 2011

Information and Communication Technology (ICT) infrastructure for collaboration with regional universities and colleges, and management are discussed. The infrastructure consisted of Moodle servers at each institution, Moodle Lite, backup servers, test servers, a Video On Demand (VOD) server, a video meeting system, and other supporting systems. ICT infrastructure was designed and managed by a committee in charge of the collaboration. Members of the committee consisted of fifteen faculty members from each institution in the collaboration. Five technical support staff members were employed for managing the infrastructure. © 2011 ACM.

Kurata R.,Japan National Agricultural Research Center | Yahara S.,Kumamoto University | Yamakawa O.,Japan National Agricultural Research Center | Yoshimoto M.,Japan National Agricultural Research Center | Yoshimoto M.,Kagoshima Womens Junior College
Food Science and Technology Research | Year: 2011

A simple high-yield method for purifying 3,4,5-tri-O-caffeoylquinic acid from sweetpotato leaves (Ipomoea batatas L.) was established. The method consisted of methanol extraction, water-hexane partition, MCI gel CHP20P, and Sephadex LH-20 chromatography. All purification steps required fewer than 3 days, and the yield of purified 3,4,5-tri-O-caffeoylquinic acid was calculated to exceed 76 mg from 100 g of leaf powder. Its recovery was estimated to be more than 66%, and its purity more than 98%. The aldose reductase inhibitory activities of these derivatives were 3,4,5-tri-O-caffeoylquinic acid > 3,4-di-Ocaffeoylquinic acid = 3,5-di-O-caffeoylquinic acid > 4,5-di-O-caffeoylquinic acid > 5-O-caffeoylquinic acid. These results indicate that 3,4,5-tri-O-caffeoylquinic acid is the more bioactive component, and this purification method enables in vivo experiments.

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