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Institution

Otsuma Women's University

EducationTokyo, Japan
About: Otsuma Women's University is a education organization based out in Tokyo, Japan. It is known for research contribution in the topics: Differential scanning calorimetry & Population. The organization has 422 authors who have published 913 publications receiving 12796 citations. The organization is also known as: Otsuma-Joshi-Daigaku.


Papers
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Journal ArticleDOI
TL;DR: 4-Hydroxybenzoate-polyprenyltransferase from Pseudomonas putida was partially purified by ion-exchange and gel filtration column chromatography and no inhibition was observed by the end-product, ubiquinone-9 of P. putida.
Abstract: 4-Hydroxybenzoate-polyprenyltransferase, an enzyme in ubiquinone biosynthesis, from Pseudomonas putida was partially purified by ion-exchange and gel filtration column chromatography. The enzyme required phospholipid as an essential factor for activity. Hexaprenyl pyrophosphate(-PP) and pentaprenyl-PP as well as nonaprenyl-PP were used as polyprenyl donors, but tetraprenyl- and farnesyl-PPs were scarcely transferred to 4-hydroxybenzoic acid. No inhibition was observed by the end-product, ubiquinone-9 of P. putida. Long chain acyl-CoA, free fatty acids, or isopentenyl-PP strongly inhibited the enzyme activity. A possible regulatory role of the enzyme in bacterial ubiquinone biosynthesis is discussed.

4 citations

Journal ArticleDOI
TL;DR: The results show that a highly charged polyanion is required to separate a polycation from a DNA, however, for a diblocked polyampholyte, its net dipole induces a higher probability to bridge a DNA and apolycation.

4 citations

Journal ArticleDOI
TL;DR: The physicochemical and structural changes in the dried squid during softening treatment were examined in this paper, where they were prepared at 4 or 40 °C and softened first in water and then in alkaline solution.
Abstract: Dried squid were prepared at 4 or 40 °C and softened first in water and then in alkaline solution. The physicochemical and structural changes in the dried squid during the softening treatment were examined. A significantly higher wet weight was observed for the 4 °C-dried squid during the softening treatment compared with the 40 °C-dried squid. The rupture stress and rupture energy of the 40 °C-dried squid were significantly higher than those of the 4 °C-dried squid during the softening treatment. The sodium dodecyl sulphate polyacrylamide slab gel electrophoresis (SDS-PAGE) pattern of the 4 °C-dried squid was almost the same as that of raw squid. The SDS-PAGE pattern of the 40 °C-dried squid showed many fragments of lower molecular weight. After soaking in distilled water the SDS-PAGE pattern of the 40 °C-dried squid did not change significantly; however, the SDS-PAGE pattern of the 4 °C-dried squid became the same as that of the 40 °C-dried squid. Histological analysis by light microscopy showed the formation of muscle fibre bundles in the 40 °C-dried squid. A higher water permeation was observed among the muscle fibres of the alkali-softened 4 °C-dried squid when compared with the alkali-softened 40 °C-dried squid. Copyright © 2003 Society of Chemical Industry

4 citations

Journal ArticleDOI
TL;DR: Results indicate that NIP-142 has blocking effect on the KCNQ1/KCNE1 channelCurrent, which underlies the slow component of the cardiac delayed rectifier potassium channel.
Abstract: We examined the effect of NIP-142, a benzopyran compound with terminating effect on experimental atrial arrhythmia, on the KCNQ1/KCNE1 channel, which underlies the slow component of the cardiac delayed rectifier potassium channel (IKs). NIP-142, as well as chromanol 293B, showed concentration-dependent blockade of the current expressed in HEK293 cells; the EC50 value of NIP-142 and chromanol 293B for the inhibition of tail current was 13.2 μM and 4.9 μM, respectively. These results indicate that NIP-142 has blocking effect on the KCNQ1/KCNE1 channel current.

4 citations


Authors

Showing all 423 results

NameH-indexPapersCitations
Tatsuko Hatakeyama371744301
Sakae Inouye371304270
Shigeko Hara331224300
Minatsu Kobayashi31613797
Seiichiro Aoe291633615
Motoo Arai291542669
Akira Mochizuki28802525
Tomomi Shimoikura25881903
Akira Shimatsu24652406
Shuhachi Kiriyama241082099
Yoshiyuki Koyama21661381
Ko Fujimura20401449
Masakazu Horie201011434
Shinji Sakamoto19791000
Yusuke Kanke1735779
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20231
20223
202145
202054
201954
201829