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Shozo YAMAMOTO
Article type: Article
1974 Volume 48 Issue 9 Pages
419-432
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
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Three pseudomonad monooxygenases, salicylate hydroxylase, imidazoleacetate hydroxylase and lysine oxygenase, were purified and identified to be flavoproteins. Their prosthetic flavin was flavin adenine dinucleotide. Since neither iron nor copper was detected in a significant quantity, the flavin seemed to be a sole prosthetic group of these enzymes. These and other flavooxygenases comprise a major new group of flavoproteins. Lysine oxygenase catalyzed an oxygenative decarboxylation of lysine producing an acid amide. Under anaerobic conditions, however, the enzyme showed a dehydrogenation of lysine and produced a corresponding α-keto acid. Upon the modification of the enzyme protein by sulfhydryl blocking reagents, the enzyme now catalyzed an oxidative deamination of lysine producing an α-keto acid and hydrogen peroxide. Furthermore, certain analogues such as ornithine and γ-methyllysine underwent an oxidative deamination. α-Monoamino acids were also oxidized, but only when alkylamines were present. Thus, an oxidase activity was demonstrated by the modification of either the enzyme or the substrate. The significance of this oxidase activity is discussed in terms of the oxygen activation by the flavin.
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Tadayoshi TANAKA, Kotaro MORINAGA, Shoichi MASUSHIGE, Akio MAEKAWA, Ta ...
Article type: Article
1974 Volume 48 Issue 9 Pages
433-437
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
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The growth of Saccharomyces carlsbergensis was studied when thiamine in the vitamin B_5 assay basal medium, was replaced by various thiamine-related compounds. The results were as follows ; 1) No difference was found in the growth in the medium containing thiamine diphosphate, thiamine palmitate, thiamine isovalerate, thiamine propyldisulfide, thiamine disulfide, or the mixture of 2-methyl-4-amino-5-aminomethylpyrimidine and 4-methyl-5(β-hydroxyethyl) thiazole, as compared with thiamine respectively. But the yeast growth in the medium containing O, S-dicarbethoxythiamine was lower than that in the medium containing thiamine, while, in the medium which contained ethylthiamine or chlorothiamine instead of thiamine, the state of the growth showed a high blank. 2) Ethylthiamine or chlorothiamine had no effect on the growth of thiamine-requiring Lactobacillus viridescens.
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Fumio UEDA, Tadashi HIGASHI, Yoshikazu AYUKAWA
Article type: Article
1974 Volume 48 Issue 9 Pages
439-445
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
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After estimating the swelling properties and solvent regain. values of hydroxypropylated Sephadex G-50 (organophilic dertran gel), behavior of fat-soluble vitamins on the column was examined. The available fractionation range for gel filtration utilizing hydroxypropylated Sephadex G-50 as a bed and chloroform as an eluting solvent was found to be between 200 and 10,000 in the molecular weight, but the results on the separation of fat-soluble vitamins were not better than the previous reports (Vitamins, 39,176 (1969), 40,309 (1969)) using Sephadex LH-20. Therefore, the method would be available only for separation of compounds having large differences in their molecular size.
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Shunsuke KAMISHIMA, Tadao HASEGAWA, Takao SUZUKI, Shigeru INABA
Article type: Article
1974 Volume 48 Issue 9 Pages
447-452
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
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^3H-Vitamin D_2 (^3H-D_2) and ^3H-vitamin D_2-sulfate (^3H-D_2-sulfate) were prepared by Wilzbach method and D_2-sulfate binding proteins from the rabbit intestinal mucosa and plasm were investigated in vitro. The intestinal mucosa proteins reacted with ^3H-D_2 or ^3H-D_2-sulfate, on its gel filtration using Sephadex G-200 column (1.6×70cm), were separated into six protein peaks respectively. Peak 1 equivalent to the void volume was that bound with ^3H-D_2 or ^3H-D_2-sulfate. After pronase treatment of the intestinal mucosa proteins, their binding ability with ^3H-D_2-sulfate were decreased markedly. The disk get electrophoresis of ^3H-D_2-sulfate binding proteins in the peak 1 fraction was also carried out ; all the three bands on the gel stained with amide black showed radioactivity. These results suggest that D_2-sulfate can bind with intestinal mucosa proteins to be absorbed from the intestine. When the rabbit plasm binding proteins with ^3H-D_2-sulfate were separated by gel filtration using Sephadex G-200 column, six protein peaks were observed ; the protein in peak 3 fraction was shown to be that bound with either ^3H-D_2 or ^3H-D_2-sulfate respectively.
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Kimitoshi NIGOTA
Article type: Article
1974 Volume 48 Issue 9 Pages
453-462
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
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A mutant strain of Escherichia coli, O8-442,requiring lipoic acid (LiA) for both aerobic and anaerobic growth in a minimal medium with glucose as a sole carbon source was isolated. The requirment for LiA could be replaceable by either acetate+succinate or acetate+lysine+methionine under aerobic conditions, but anaerobically it grew on either acetate or succinate alone. Pyruvate markedly stimu1ated.the respiration of the mutant cells grown aerobically on LiA and the addition of LiA did not cause a further stimulation. Conversely, results obtained with the cells grown aerobically on acetate+ lysine+methionine was quite different ; the degree of the pyruvate-oxidizing activity was very low but the activity was fully restored by the addition of LiA. In the same system, lipoamide (LiANH_2) was found to have no activity for the respiration of the mutant cells, while it was more active than LiA when extracts prepared from the mutant cells were used. These results suggest that the de novo synthesis of LiA is blocked in the mutant strain. A permeability barrier appears to be involved in the utilization of LiANH_2.
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
463-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
463-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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Upendra Prasad C, M.Bose S
Article type: Article
1974 Volume 48 Issue 9 Pages
463-464
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
464-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
FREE ACCESS
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[in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
464-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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V.Khandwekar P, Nath N, C.Nath M
Article type: Article
1974 Volume 48 Issue 9 Pages
464-465
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
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Migasena Panata, I.Thurnham D, Pongpaew Praneet, Hongthong Kanjana, Ha ...
Article type: Article
1974 Volume 48 Issue 9 Pages
465-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
465-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
465-
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
465-466
Published: September 25, 1974
Released on J-STAGE: March 14, 2018
JOURNAL
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
467-
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
JOURNAL
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[in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
468-
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
JOURNAL
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[in Japanese], [in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
468-469
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
JOURNAL
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[in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
469-
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
JOURNAL
FREE ACCESS
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[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1974 Volume 48 Issue 9 Pages
469-470
Published: September 25, 1974
Released on J-STAGE: March 02, 2018
JOURNAL
FREE ACCESS