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Volume 62, Issue 8
Displaying 1-31 of 31 articles from this issue
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Shigeru ONOArticle type: Article
1988 Volume 62 Issue 8 Pages 375-383
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSFAD, as one of the ester-forms of riboflavin, is formed by FAD pyrophos-phorylase from FMN and plays an important role as a coenzyme in the oxidoreduction system. Various physiological actions of FAD have been investigated using rats. The induction of adrenal atrophy in rats treated with dexamethasone phosphate was partially prevented by the simultaneous administration of FAD. Electronmicroscopic study showed that the number of organelles and fat droplets, the shape of the nuclei in the fascicular zone, the decrease of glucose-6-phosphate dehydrogenase activity and the turnover of ^<32>P in the cell fractions of adrenals were normalized by FAD administration compared to dexamethasone alone. The ^<32>P turnover in the adrenal-microsomal fraction in the dexamethasone treated rats increased remarkably by simultaneous administration of FAD and ACTH. The finding suggests a synergistic effect between FAD and ACTH. The decreased synthesis of cortisol-binding protein in the lens by dexamethasone phosphate was restored by FAD administration probably due to promotion of mRNA turnover. The stimulation effect of in vitro FAD on rat lenticular glutathione reductase represents a sensitive indicator of the riboflavin nutritional status as well as the activity coefficient of glutathione reductase in human and rat erythrocyte.View full abstractDownload PDF (1316K) -
Toshiharu NAGATSU, Sadao MATSUURA, Takashi SUGIMOTOArticle type: Article
1988 Volume 62 Issue 8 Pages 385-392
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSThe biochemical activity of natural 6R-form of tetrahydrobiopterin was compared with that of the unnatural 6S-form in terms of the all pterin-requiring monooxygenases, phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase. The unnatural (6S)-isomer showed some comparable in vitro cofactor activities as the natural (6R)-isomer towards the three monooxygenases. How-ever, the natural (6R)-isomer showed a marked in situ or in vivo activities, whereas the unnatural (6S)-isomer had almost no activities. These results suggest that only the natural (6R)-isomer may have in vivo biological activities.View full abstractDownload PDF (773K) -
Toshiyuki SAKANO, Shigeru NOTSUMOTO, Tadayoshi NAGAOKA, Atsushi MORIMO ...Article type: Article
1988 Volume 62 Issue 8 Pages 393-398
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSVitamin K_1 (K_1) and vitamin K_2 (MK-n) in foods were measured by a method based on high-performance liquid chromatography (HPLC) combined with chemical reduction and fluorometric detection. The vitamins extracted from foods were purified with a silica SEP-PAK cartridge and/or thin-layer chromatography (TLC) and a silica SEP-PAK cartridge followed by TLC, respectively, and then measured by using an HPLC system. More than 1μg/g or ml of K_1 was found in salad oil, spinach leaf, green welsh onion, broccoli, purple laver, hijiki, wakame, green tea and black tea, and MK-n was mainly found in fermented foods.View full abstractDownload PDF (551K) -
Hiroshi TAGUCHI, Kunikatsu INAMORI, Hideya MUTO, Katsuzumi OKUMURA, Yo ...Article type: Article
1988 Volume 62 Issue 8 Pages 399-406
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDistribution of nicotinamidase (EC 3. 5. 1.19) was investigated in 150 kinds of samples of animals, plants and microorganisms. In general, very high activities were detected in mushrooms and marine products. Relatively high activities were found in microorganisms. The enzyme activity was not detected or very low in mammals and leaves of trees. A close relationship in the distribution was observed between this enzyme and nicotinate methyltransferase (EC 2. 1. 1. 7). Fundamental properties of nicotinamidase in the cell-free extract of several samples were compared. Namely, the optimum pH for the reaction was 6.9〜9.8 and Km values for nicotinamide at each opt mum pH were 1.2〜5.9μM. Heavy metal ions, quinolinic acid, nicotinic acid (product inhibition) were found to be potent inhibitors for partially purified nicotinamidase from "Tora-makitake" mushroom.View full abstractDownload PDF (719K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 407-408
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (172K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 409-416
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (685K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...Article type: Article
1988 Volume 62 Issue 8 Pages 417-424
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
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[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 425-432
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
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[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 433-437
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (529K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 439-445
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (887K) -
Article type: Appendix
1988 Volume 62 Issue 8 Pages 447-450
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
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[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 451-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (181K) -
[in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 451-452
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (320K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 452-453
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (320K) -
[in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 453-454
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (305K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 454-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (176K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 455-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (158K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...Article type: Article
1988 Volume 62 Issue 8 Pages 455-456
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (302K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...Article type: Article
1988 Volume 62 Issue 8 Pages 456-457
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (329K) -
[in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 457-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (186K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 457-458
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (314K) -
[in Japanese], [in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 459-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (185K) -
[in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 459-460
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (330K) -
[in Japanese], [in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 460-461
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (322K) -
[in Japanese], [in Japanese], [in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 461-462
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (204K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 463-464
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (295K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 464-
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (178K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 464-465
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (307K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 465-466
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (289K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 467-468
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (268K) -
[in Japanese]Article type: Article
1988 Volume 62 Issue 8 Pages 468-469
Published: August 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL FREE ACCESSDownload PDF (297K)
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