1 0 0 0 OA 腹式呼吸

著者
二木謙三 著
出版者
文星堂[ほか]
巻号頁・発行日
1911
著者
志々田 文明
出版者
早稲田大学人間科学学術院
雑誌
人間科学研究 = Waseda journal of human sciences (ISSN:09160396)
巻号頁・発行日
vol.第3巻, no.第1号, pp.161-171, 1990
著者
渡邊 精一
出版者
日本甲殻類学会
雑誌
Cancer : 会員連絡誌 (ISSN:09181989)
巻号頁・発行日
vol.6, pp.37-40, 1997-05
参考文献数
10
被引用文献数
6
著者
堀本柵 (楓仙子) 著
出版者
学友館
巻号頁・発行日
1895
著者
中村 吉三郎
出版者
早稲田大学法学会
雑誌
早稲田法学 (ISSN:03890546)
巻号頁・発行日
vol.43, no.1-2, pp.115-129, 1968-03-20
著者
Chikako YAMADA Hidehiko IZUMI Junko HIRANO Aya MIZUKUCHI Mitsuo KISE Tsukasa MATSUDA Yasuko KATO
出版者
(社)日本農芸化学会
雑誌
Bioscience, Biotechnology, and Biochemistry (ISSN:09168451)
巻号頁・発行日
vol.69, no.10, pp.1877-1883, 2005 (Released:2005-10-23)
参考文献数
28
被引用文献数
16

The effect of germination and subsequent heat-processing on the degradation of soluble proteins, including some allergenic proteins, in brown rice grains was investigated. The content of soluble proteins, including 14–16-kDa and 26-kDa allergens, in the germinated and processed brown rice grains (GPR) was much lower than that of non-germinated brown rice. These proteins in brown rice grains were also much lower after subsequent heat-processing during the manufacturing process. The protease activity of germinated brown rice (GR) was detected and increased 1.5 times after germination. The optimum pH values for degradation of the 26-kDa and 14–16-kDa allergens in the GR grains were 4 and between 5 and 7, respectively. These results suggest that the decrease in the soluble proteins and allergens was induced in part by proteolytic degradation. The presence of a detergent enhanced the proteolytic degradation of the soluble proteins, especially of the 26-kDa allergen, in the brown rice grains. The degradation of the 26-kDa allergen was weakly inhibited by NEM, suggesting cysteine protease(s) may have been involved in its degradation. These results suggest that the two abundant allergens were degraded in a different manner and probably by different proteases in the grains during germination.
著者
右田 たい子 吉田 匡
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.44, no.2, pp.81-86, 2004 (Released:2004-03-23)

Plant heme oxygenase (HO), which catalyzes conversion of heme to biliverdin, being further converted to photo-receptive phycobilins, had been known only in the cell extracts of primitive red algae and cyanobacteria for these twenty years. Recent development of gene analysis, however, has shown that HO is ubiquitously contained in variety of living species. We have succeeded for the first time in obtaining recombinant HO protein of cyanobacteria and in characterizing the HO protein and its heme complex by spectroscopic analyses. Here, we review the existence, role, and characteristics of cyanobacterial and plant HOs in comparison with those of mammalian and bacterial HOs.

1 0 0 0 OA 手風琴独案内

著者
箸尾竹軒 著
出版者
青木嵩山堂
巻号頁・発行日
vol.[第1集], 1894

1 0 0 0 OA 鑑薬精義

著者
石塚左玄 著
出版者
陸軍文庫
巻号頁・発行日
vol.1, 1876

1 0 0 0 OA [絵本]

著者
仮名垣魯文 (猫々道人) 編
出版者
金松堂
巻号頁・発行日
vol.〔3〕 高橋阿伝夜叉譚 5編 上, 1880

1 0 0 0 OA [絵本]

著者
荒川吉五郎 編
出版者
荒川吉五郎
巻号頁・発行日
vol.〔10〕 小栗判官一代記 下, 1882

1 0 0 0 OA 蘭学大道編

著者
佐藤信淵 著
出版者
報効義会
巻号頁・発行日
1920

1 0 0 0 OA 千島探験

著者
笹森儀助 編
出版者
笹森儀助
巻号頁・発行日
1893

1 0 0 0 OA 新女子道

著者
内田節三 (節堂) 著
出版者
伸文社[ほか]
巻号頁・発行日
1911