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| 1.
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田崎, 和江 ; Tazaki, Kazue
概要:
金沢大学理工研究域地球社会基盤学系<br />Nitrogen both in the recent and fossil shells were analysed by micro-Kjeldahl method, the latter
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being from the Johmon shell-mounds (2000-9000 years B.P.) in the Kanto district, Japan. It is difficult to separate the organic metrials from calcium carbonate without any loss especially in the fossil shells, so the nitrogen analysis of the shell should be carried out with much calcium carbonate, not to remove it. The writer is successful in quantitative nitrogen analysis of the organic materials with much calcium carbonate (Fig. 1). Both the fossil and recent samples analysed are Anadara broughtoni, A. subcrenata, Ostrea gigas, Corbicula iaponica, C. leana, Meretrix lusoria, Mya japonica and Neverita didyma, which are shown in Table 1 with places of occurrence, absolute ages, and weight percents of nitrogen in the shell. In so far as the fossil shells of the Johmon shellmounds are concerned, it is concluded that nitrogen content of the shell indicates rapid diminishing in 2000 years and slow decreasing since then (Fig. 2).
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| 2.
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出石, 隆 ; 鏑木, 光朗 ; 玉鉾, 良三 ; 米谷, 数子 ; 中原, 吉晴 ; 能崎, 克巳 ; 竹内, 昭 ; 亀田, 富子 ; 松扉, 繁麿 ; 小倉, 幸春
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| 3.
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田辺, 啓三 ; 幸山, 彰一 ; 光谷, 音吉 ; 高瀬, 允 ; 竹内, 昭 ; 松扉, 繁麿 ; 野々市, 幸子 ; 亀田, 富子 ; 出石, 隆
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| 4.
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米谷, 数子
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| 5.
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中原, 吉晴
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| 6.
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幸山, 彰ー ; 亀田, 富子
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| 7.
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鏑木, 光朗
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| 9.
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Itagaki, Eiji ; Fujita, Takeshi ; Sato, Ryo ; 板垣, 英治
概要:
A preparation containing formate dehydrogenase, cytochrome b1 and nitrate reductas_??_ was solubilized and partially purified from the particulate fraction of E. coli cells growr_??_ anaerobically under the conditions favorable
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for nitrate respiration. Some properties o_??_ formate dehydrogenase and cytochrome b1 in this purified preparation were investigated It was suggested that formate dehydrogenase is a metalloflavoprotein with essential sulf_??_ hydryl groups. Its activity was strongly bu_??_ reversibly inhibited by molecular oxyge_??_ The prosthetic group of cytochrome b1 was decisively identified as protoheme, and it was found that the cytochrome is autoxidizable. The reduction of cytochrome b1 by formate was shown to require, in addition to formate dehydrogenase, a lipid-soluble factor which could be replaced by vitamin K3 in the solubilized system.We are indefted to Drs. H. Maeno and S. Sakakibara for generous gifts of crude snake venonand crystalline protohemin, respectively.
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| 10.
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Fujita, Takeshi ; Itagaki, Eiji ; Sato, Ryo ; 板垣, 英治
概要:
Cytochrome b1 was solubilized from the particulate fraction of Escherichia coli with the aid of snake venom and deoxycho
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late and was extensively purified by ammonium sul-fate fractionation and hydroxylapatite column chromatography. The purifed preparation was still contaminated by a colorless impurity which sedimented more slowly than the cytochrome in the ultracentrifugal field; the purity being estimated to be 50 to 70 per cent. A molecular weight of 600, 000 to 800, 000 could be expected for the cytochrome from its sedimentation constant. On the other hand, aminimum molecular weight of about 160, 000 was obtained from the heme content of the cytochrome. The cytochrome could be split by acid acetone into protoheme and an apoprotein moiety. The recombination of the two components could be observed spectro-photometrically, but the reconstructed cytochrome was no more native as evidenced by its capabiliiy to combine with CO. The normal oxidation-reduction potential of purified cytochrome bt was determined to be about -20 mV at pH 7.0 and 25°C. Spectral properties, reactivity and chemical composition of the purified preparation were also studied.We wish to thank Dr. A. Ohsaka of the Natio-nal Institute of Health, Tokyo, for a generous gift of snake venom, and Dr. K. Kakiuchi of the Institute for Protein Research, Osaka University, Osaka, for carrying out the ultracentrifugal analyses.
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| 11.
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Itagaki, Eiji ; Fujita, Takeshi ; Sato, Ryo ; 板垣, 英治
概要:
The reactions of cytochrome b1 and nitrate reductase in an enzyme preparation solubiliz-ed and partially purified from the particulate fraction of Escherichia coli were investigated. The cytochrome b1 reduced by the addition of formate and
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vitamin K3 was found to be reoxidizable by oxygen, nitrate and chlorate. While the oxidation by oxygen was insensitive to cyanide and azide (the autoxidizability of the cytochrome), these reagents strongly inhi-bited the reaction by nitrate and chlorate suggesting the intervention of nitrate reduc-tase. With chlorate as the oxidant, the de-formation of the absorption spectrum of the cytochrome was observed. The nitrate reduc-tion by formate in the solubilized system was found to require the addition of vitamin K3, but flavins had no effects on this reaction. Since the vitamin is required also for thereduction of cytochrome b1 in this prepara-tion, the involvement of the cytochrome in the nitrate-reducing mechanism was further substantiated. The formate-nitrate reaction was strongly inhibited by 2-heptyl-4-hydroxy-quinoline-N-oxide (HOQNO), but this inhibi-tion was not competitive with respect to vitamin K3. It was spectrophotometrically revealed that HOQNO inhibits the reoxidation of cytochrome bt by nitrate, but not the re-duction by formate plus vitamin K3. In the particulate fraction, the formate-nitrate reduc-tase activity was inhibited much more remark-ably than the formate oxidase activity. Some of the implications of these results are dis-cussed.We wish to thank Dr. S. Taniguchi for a gener-ous gift of 2-heptyl-4-hydoxyquinoline-N-oxide.
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| 12.
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Itagaki, Eiji ; 板垣, 英治
概要:
A pale-brown powder preparation of the particulate fraction of E. coli cells grown with nitrate respiration was obtained with cold acetone treatment. This preparation, was similar to the solubilized and partially purified enzyme
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preparation, had high activities of for-mate dehydrogenase and nitrate reductase and contained cytochrome b1, but no activity of formate-nitrate reductase system. By addition of lipids prepared from this organism with aid of a detergent, PADA, the activity of formate-nitrate reductase system was completely restored. The restoration efficiencies of enzyme activity by UQ8 and K2 which were quinones found in this organism, were 2.6 to 1 per mole.The experiments with the UQ8, K2 or both specifically deprived, and ultraviolet irradiated lipid preparations showed that UQ8, rather than K2, acted more effectively as an electron carrier.UQ8 was anaerobically reduced slowly by the enzyme preparation wit formate, and UQ8H2 was rapidly oxidized by nitrate with simultaneous production of stoichiometric amounts of nitrite. From these results, it is concluded taht UQ8 acts principally as hydrogen acceptor for formate dehydrogenase of E. coli.The author is very grateful to Professer R. Sato of this laboratory for his helpful advice, to Mr. T. Fujita of his continous discussion to this work, to Dr. S. Ikeda of the Faculty of Science, Osaka University for his helpful advice to the synthesis of PADA, to Dr. K. Tanaka of Takeda Pharmaceutical Industries Ltd., Osaka and Dr. K. Uehara of the Pharmac-eutical Faculty of Osaka University for materials, and to Dr. K. Kusai of Nagase Sangyo Co. Ltd. for large culture of the organism.
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| 13.
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Itagaki, Eiji ; Suzuki, Sakaru ; 板垣, 英治
概要:
An enzymatic method is described for the estimation of formic acid formed during the periodate oxidation of carbohydrate
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s in the 10-2μmole range. The method is based on the coupled action of formic acid dehydro-genase and nitrate reductase obtained as a particulate fraction from Escherichia coli strains. The enzymes catalyze the quantitative reduc-tion of nitrate with formic acid to yield nitrite. The nitrite is estimated by a photometric me-thod. The results obtained using this method on D-glucose, L-rhamnose, N-acetyl-D-glucos-amine and UDP-glucose are given.The authors express their thanks to Mr. M. Iwatsuka for his technical assistance.
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| 14.
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Sugawara, Masayuki
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| 15.
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Miyashita, Kenzo
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| 16.
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日南田, 一男
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| 17.
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最上, 雄文
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| 18.
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井崎, 宏一
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| 19.
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金子, 直一
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| 20.
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田中, 宏幸
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| 21.
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提山, 淑郎
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| 22.
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大滝, 敏夫
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| 23.
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藤平, 悳郎
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| 24.
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内田, 洋
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| 25.
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三浦, 元俊
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| 26.
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鈴木, 直治
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| 27.
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笹本, 正治
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| 28.
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笹本, 正治 ; 東, 正子 ; 木戸, 喜一 ; 幸山, 彰一 ; 盛, 大衛
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| 29.
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関, 雅美
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| 30.
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室木, 弥太郎
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| 31.
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室木, 弥太郎
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| 32.
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原, 栄一
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| 33.
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輪島, 士郎
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| 34.
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桑野, 英正
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| 35.
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橘, 好一
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| 36.
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Fukuda, Shozo
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| 37.
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Sugawara, Masayuki
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| 38.
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最上, 雄文
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| 39.
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金子, 直一
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| 40.
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田中, 宏幸
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| 41.
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藤平, 悳郎
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| 42.
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松原, 雅典
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| 43.
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鈴木, 直治
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| 44.
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笹本, 正治 ; 東, 正子 ; 木戸, 喜一 ; 幸山, 彰一 ; 盛, 大衛
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| 45.
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宮下, 健三
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| 46.
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輸島, 士郎
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| 47.
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井出, 弘之
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| 48.
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山田, 琢
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| 49.
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森野, 宗明
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| 50.
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室木, 弥太郎
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| 51.
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Nagai, Yoshio
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| 52.
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Shimizu, Chujiro
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| 53.
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Izaki, Koichi
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| 54.
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Sugawara, Masayuki
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| 55.
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Tachibana, Yoshikazu
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| 56.
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柿本, 典昭
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| 57.
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日南田, 一男
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| 58.
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金子, 直一
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| 59.
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田中, 宏幸
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| 60.
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南, 次郎
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| 61.
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大滝, 敏夫
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| 62.
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三浦, 元俊
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| 63.
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松原, 雅典
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| 64.
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笹本, 正治 ; 東, 正子 ; 木戸, 喜一 ; 幸山, 彰一 ; 盛, 大衛
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| 65.
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輪島, 士郎
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| 66.
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山田, 琢
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| 67.
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室木, 弥太郎
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| 68.
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森野, 宗明
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| 69.
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輪島, 士郎
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| 70.
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Shimizu, Chujiro
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| 71.
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Sugawara, Masayuki
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| 72.
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Miyashita, Kenzo
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| 73.
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多田, 治夫
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| 74.
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日南田, 一男
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| 75.
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井崎, 宏一
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| 76.
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吉安, 光徳
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| 77.
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洲崎, 恵三
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| 78.
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金子, 直一
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| 79.
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松原, 雅典
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| 80.
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笹本, 正治 ; 東, 正子 ; 木戸, 喜一 ; 盛, 大衛
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| 81.
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山田, 藤次郎
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| 82.
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最上, 宏信
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| 83.
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山田, 琢
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| 84.
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室木, 弥太郎
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| 85.
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金沢大学教養部
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| 86.
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Tasda, Haruo
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| 87.
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Shimizu, Chujiro
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| 88.
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Oba, Kiyoshi
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| 89.
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Wajima, Shiro
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| 90.
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福田, 尚造
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| 91.
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日南田, 一男
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| 92.
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井崎, 宏一
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| 93.
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井出, 弘之
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| 94.
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金子, 直一
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| 95.
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山田, 杉夫
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| 96.
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三浦, 元俊
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| 97.
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鈴木, 直治
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| 98.
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山田, 藤次郎
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| 99.
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大滝, 敏夫
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| 100.
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最上, 宏信
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