VITAMINS
Online ISSN : 2424-080X
Print ISSN : 0006-386X
Volume 72, Issue 3
Displaying 1-8 of 8 articles from this issue
  • Katsumi SHIBATA
    Article type: Article
    1998 Volume 72 Issue 3 Pages 85-96
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    The feeding on a diet containing thyroxine to rats significantly increased the conversion ratio of tryptophan to niacin, while, the feeding on a diet containing estrone decreased. The feeding on a diet containing progesterone or testosterone did not affect the conversion ratio. An intraperitoneal injection of adrenaline, alloxan, or streptozotocin caused the decreased conversion ratio. The intraperitoneal injection of prednisolone, a synthetic adrenal cortical hormone, increased the conversion ratio after 1 day ; however, the conversion ratio was lower in the prednisolone group than in control group after 3, 4, 5 and 6 days. On around 7th day, the conversion ratio was restored to the control values. The target of these hormones, by which the conversion ratio was affected, was the activity of liver aminocarboxymuconate-semialdehyde decarboxylase. Thus, the metabolism of tryptophan to niacin is found to be regulated and controlled by the activity of aminocarboxymuconate-semialdehyde decarboxylase via thyroid gland, adrenal, pancreas, and ovary hormones.
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  • Hiroyuki KAGAMIYAMA
    Article type: Article
    1998 Volume 72 Issue 3 Pages 97-106
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Pyridoxal enzymes catalyze versatile reactions with amino acids, including transamination, recemization, α, β-elimination, and decarboxylation. The reaction mechanism for these reactions has been explained on the basis of diverse chemical properties of pyridoxal phosphate. Recent progress in recombinant DNA techniques allowed us to examine the role of apoproteins of the pyridoxal enzymes at the atomic level based on crystallographic and sitedirected mutagenesis studies. Among the pyridoxal enzymes, aminotransferases, particularly aspartate aminotransferase, have been most extensively studied from structural and functional aspects. In this paper, I will describe some important information obtained recently on substrate recognition and transaldimination, which are the initial steps common to all the pyridoxal enzymes, centering discussion on the uniqueness of aspartate aminotransferase.
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  • Article type: Bibliography
    1998 Volume 72 Issue 3 Pages 107-110
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
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  • [in Japanese], [in Japanese]
    Article type: Article
    1998 Volume 72 Issue 3 Pages 111-112
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Download PDF (316K)
  • [in Japanese]
    Article type: Article
    1998 Volume 72 Issue 3 Pages 112-113
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Download PDF (327K)
  • [in Japanese]
    Article type: Article
    1998 Volume 72 Issue 3 Pages 113-114
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Download PDF (331K)
  • [in Japanese]
    Article type: Article
    1998 Volume 72 Issue 3 Pages 114-115
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Download PDF (311K)
  • [in Japanese]
    Article type: Article
    1998 Volume 72 Issue 3 Pages 115-118
    Published: March 25, 1998
    Released on J-STAGE: December 26, 2017
    JOURNAL FREE ACCESS
    Download PDF (411K)
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