Institution
Otsuma Women's University
Education•Tokyo, 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.
Topics: Differential scanning calorimetry, Population, Glass transition, Cardiopulmonary resuscitation, Bound water
Papers published on a yearly basis
Papers
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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
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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
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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
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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
Name | H-index | Papers | Citations |
---|---|---|---|
Tatsuko Hatakeyama | 37 | 174 | 4301 |
Sakae Inouye | 37 | 130 | 4270 |
Shigeko Hara | 33 | 122 | 4300 |
Minatsu Kobayashi | 31 | 61 | 3797 |
Seiichiro Aoe | 29 | 163 | 3615 |
Motoo Arai | 29 | 154 | 2669 |
Akira Mochizuki | 28 | 80 | 2525 |
Tomomi Shimoikura | 25 | 88 | 1903 |
Akira Shimatsu | 24 | 65 | 2406 |
Shuhachi Kiriyama | 24 | 108 | 2099 |
Yoshiyuki Koyama | 21 | 66 | 1381 |
Ko Fujimura | 20 | 40 | 1449 |
Masakazu Horie | 20 | 101 | 1434 |
Shinji Sakamoto | 19 | 79 | 1000 |
Yusuke Kanke | 17 | 35 | 779 |