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Sachiko YAMADA
Article type: Article
1996 Volume 70 Issue 2 Pages
43-55
Published: February 25, 1996
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This review comprises of three parts : metabolism of vitamin D_3, syntheses of vitamin D metabolites, and syntheses of vitamin D analogs. In the first part, the in vitro as well as in vivo metabolism of 24,25(OH)_2D_3, the biosynthetic pathway of 25-OH-D_3 26,23-lactone, and the metabolism of vitamin D at the conjugated triene part are briefly discussed. In the second part, facile stereoselective method for introducing various structure of the side chains of vitamin D metabolites and syntheses of those side chain modified metabolites are described. Also a facile method for labeling deuterium or tritium at the 6- and 19-positions of vitamin D via its SO_2 adduct is described. In the third part, syntheses and biological implications of various vitamin D analogs are briefly discussed that include 1α-OH-D_3, 24,24-difluorovitamin D_3 analogs, and conformationally restricted analogs designed to study vitamin D conformation responsible for binding to VDR(vitamin D receptor).
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Yoshitaka TAKAHASHI
Article type: Article
1996 Volume 70 Issue 2 Pages
57-66
Published: February 25, 1996
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Two types of arachidonate 12-lipoxygenase which catalyze the transformation of arachidonic acid to 12(S)-hydroperoxy-5,8,10,14-eicosatetraenoic acid have been classified into leukocyte-type and platelet-type in terms of their substrate specificities, immunogenicities, primary structures and gene organizations. The leukocyte-type enzyme has been found not only in leukocytes but also in bovine tracheal epithelium, porcine anterior pituitary, canine brain and rat pineal gland. Recently the platelet-type enzyme was also found in tissues other than platelets. Human and mouse epidermal cells as well as human epidermoid carcinoma A431 cells contain a platelet-type enzyme. The leukocyte enzyme oxygenates not only free polyenoic acids but also more complex substrates such as phospholipids and lipoproteins. The finding that 12-lipoxygenase transforms low density lipoprotein to its oxidized form suggests the possible involvement of this enzyme in the pathogenesis of atherosclerosis. The platelet enzyme reacts with leukotriene A_4 to produce bioactive compounds, lipoxin A_4 and B_4.
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Shinji SHIMIZU
Article type: Article
1996 Volume 70 Issue 2 Pages
67-75
Published: February 25, 1996
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Flavokinase (ATP : riboflavin 5'-phosphotransferase, EC 2. 7. 1. 26, FK) was purified from chicken liver by gel filtration on Sephadex G-50 and affinity chromatography. The specific activity of the enzyme was 760 units/mg of protein. The enzyme was purified approximately 1,000-fold from the supernatant of the crude extract. The apparent molecular weight of the enzyme was calculated to be 14,000±1,000 by gel filtration on TSKgel G3000SW, and to be 13,500±1,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimal temperature of the reaction was lower than that of FK from rat liver and small intestine. The optimal pH was 9.0 for 10^<-4>M Zn(II) and 9.6〜for 10^<-4>M Mg(II). The purified FK showed the activity with ATP as the phosphate donor. No activity was observed with GTP, CTP, ADP, and AMP, as opposed to finding for the rat small intestine FK which was active with UTP as effective as ATP. The K_m value for ATP was calculated to be approximately 20 μM. The K_i value for ADP was calculated to be 200 μM against ATP. This K_i value was approximately 9 times as large as that of the rat liver FK reported by Yamada et al. The isoelectric point was determined to be approximately 5.7. The enhancement of FK activity attributable to addition of riboflavin binding protein was not confirmed.
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
77-
Published: February 25, 1996
Released on J-STAGE: December 26, 2017
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
77-78
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
78-79
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
80-
Published: February 25, 1996
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[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
Article type: Article
1996 Volume 70 Issue 2 Pages
80-81
Published: February 25, 1996
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[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
Article type: Article
1996 Volume 70 Issue 2 Pages
81-82
Published: February 25, 1996
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[in Japanese], [in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
83-84
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
84-
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
84-85
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
86-
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
86-87
Published: February 25, 1996
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
87-88
Published: February 25, 1996
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[in Japanese], [in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
88-89
Published: February 25, 1996
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[in Japanese], [in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
89-90
Published: February 25, 1996
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[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
Article type: Article
1996 Volume 70 Issue 2 Pages
90-91
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
91-92
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
93-94
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
94-95
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
96-
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
96-98
Published: February 25, 1996
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[in Japanese]
Article type: Article
1996 Volume 70 Issue 2 Pages
98-100
Published: February 25, 1996
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