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Volume 47 (1960)
- Issue 6 Pages 699-
- Issue 5 Pages 559-
- Issue 4 Pages 401-
- Issue 3 Pages 273-
- Issue 2 Pages 145-
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Volume 47, Issue 3
Displaying 1-15 of 15 articles from this issue
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I. GLUTAMATE FORMATION AND ITS RELATED ENZYMES IN BREVIBACTERIUM FLAVUM, No. 2247ISAMU SHIIO1960 Volume 47 Issue 3 Pages 273-282
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. α-Ketoglutarate or glutamate (in the presence of ammonium ions) was formed aerobically from acetate by resting cells of Brevibacterium flavum, No. 2247.
2. When C14-carbon dioxide was added to the latter reaction system, glutamate formed was labelled almost exclusively in the α-carboxyl carbon.
3. Reactions of acetate were studied in cell-free extracts of this bacterium. Such extracts are capable of catalysing the formation of acetyl-CoA from acetate, presumably via acetyl-phosphate.
4. Acetyl-CoA thus formed reacts both with oxaloacetate, to form citrate, and with glyoxylate to form malate.
5. Evidence for the presence of DPN-specific malic dehydrogenase and TPN-specific malic enzyme was obtained with cell-free extracts.
6. From these results, a probable pathway of glutamate formation from acetate was proposed.
The authors are indebted to Prof. F. Egami of the University of Nagoya, Prof. S. Akabori of the Osaka University, and Dr. H. Oeda, Mr. N. Motozaki and Mr. T. Tsunoda of our laboratory for the helpful criticism and encouragement during the course of this work.View full abstractDownload PDF (626K) -
III. PURIFICATION AND PROPERTIES OF THIAMINOKINASE FROM RAT LIVERYOSHITAKE MANO1960 Volume 47 Issue 3 Pages 283-289
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThiaminokinase from rat liver was purified about 120 fold compared with the extract from acetone-dried powder and the method for its preparation was described. The purification consisted of the following six steps: 1) Preparation of acetone-dried powder, 2) extraction with 0.05M Tris buffer of pH 7.8, 3) heat treatment at 52° for 5 minutes at pH 5.8, 4) ammonium sulfate fractionation (0.52 to 0.68 saturation), 5) acid treatment at pH 4.3 for 30 minutes at 37°, and 6) alumina Cγ-gel column chromatography with phosphate buffer of various concentrations as a elution system. The enzyme was stable between pH 7.2 and 5.8, and showed a considerable resistance to acid treatment. The preparation derived from the last step showed about 68 per cent purity by electrophoresis and was practically free from the activities of adenylate kinase, ATPase, nucleoside diphosphokinase, and thiamine pyrophosphatase. Some descriptions on its properties were also made in brief.
The author's thanks are due to Prof. N. Shimazono for his guidance and encouragement during the course of this work.View full abstractDownload PDF (434K) -
THEIR FORMATION AND LOCALIZATION ON CELLULAR COMPONENTSKOITI TITANI, SHIGEKI MINAKAMI, HIROMI MITSUI1960 Volume 47 Issue 3 Pages 290-302
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Cytochromes of Pseudomonas-P were studied by the opal glass method. Pseudomonas-P had cytochromes 553 and 560. Cytochrome 553 was extracted and partially purified.
2. Cytochrome content in Pseudomonas-P varied remarkably in response to the growth phase and as well as to the growth medium.
3. The distribution of cytochromes on cellular components of Pseudomonas-P was examined. Both of cytochromes 553 and 560 were the most abundant in SP (small particle) fraction.
4. The incorporation of racioactive iron into growing cells of Pseudomonas-P and the distribution of radioactivity taken up on the cellular components were examined. The results were discussed in relation to the observations on cytochrome formation and localization.
5. The incorporation of radioactive iron into heme by the washed cells, the disrupted cells or the cellular components of Pseudomonas-P was examined. Of the cellular components, LP (large particle) fraction was the most active in the iron incorporation.
The authors express their thanks to Prof. S. Akabori and Prof. H. Yoshikawa for their interests during the course of this work. Thanks are also due to Dr. K. Shibata for his aid in the application of his opal glass method to this work.View full abstractDownload PDF (765K) -
II. ENZYMATIC PHOSPHORYLATION OF NUCLEOSIDESHIDEO KATAGIRI, HIDEAKI YAMADA, KAZUTAMI IMAI1960 Volume 47 Issue 3 Pages 303-306
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. It was shown that G-1-P phosphotransferase of E. coli catalyzed the transphosphorylation from G-1-P to nucleosides, synthesizing the corresponding nucleotides.
2. The experimental results using adenosine, indicated that the enzyme specifically phosphorylated the 5'-position of sugar moiety of nucleoside.
3. A possible role of G-1-P phosphotransferase in the biosynthesis of nucleotides was discussed.View full abstractDownload PDF (248K) -
III. ON THE AMINO-TERMINAL PEPTIDE OF BACTERIAL AMYLASEKIN-ICHI SUGAE, YOSHIHIDE HONDA1960 Volume 47 Issue 3 Pages 307-314
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe N-terminal peptides of DNP-bacterial amylase were obtained by partial hydrolysis with concentrated hydrochloric acid and Streptorryces protease G. The amino acid sequence of the N-terminal DNP-peptide is proposed to be Val-Asp•[or Asp (NH2)]-Gly-Glu•[or Glu (NH2)]-Ser-(Ala, Val, Leu or Ileu)•••. This result teas discussed in comparison with that of Taka-amylase A.
We would like to express gratitude to Prof. S. Akabori for his kind guidance throughout this investigation and also to Nagase Ltd. Co. for the gift of bacterial amylase and to Dr. M. Nomoto for the supply of Streptomyces protease G.View full abstractDownload PDF (447K) -
NIKICHI OKUMURA, SABURO OTSUKI, AKIRA KAMEYAMA1960 Volume 47 Issue 3 Pages 315-320
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The analysis of amino acids in the protein-free extracts of the human brain has been carried out by means of ion exchange chromatography.
2. The various areas of brains were obtained from the individual dying of accident and from fetuses on the fifth and eighth gravid months. Four fresh brain tissues were obtained during the surgical operation in the patients with cerebral tumors or with epilepsy.
3. In general the distribution pattern of the free amino acids in the various areas of the human brains resembled that in dog. γ-Aminobutyric acid was detected in a large amount in the globus pallidus and the hypothalamus.
4. The quantities of free amino acids in the fetal brains differ significantly from those in the mature human brain. Taurine and phosphoethanolamine were detected in a larger amount and glutamic acid, aspartic acid, γ-amino-butyric acid and N-acetylaspartic acid were less.
5. In the brains from brain tumors there was a considerable amount of cystathionine. In the brains of accidental death and of epilepsy this substance was far less. In the fetal brains this could hardly be recognized.View full abstractDownload PDF (366K) -
TAIJIRO MATSUSHIMA, TOKUJI IKENAKA, SHIRO AKABORI1960 Volume 47 Issue 3 Pages 321-325
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA several cysteic acid peptides were separated from the partial hydrolysate of oxidized Taka-amylase A through column chromatography of Dowex-2 and the structure of the following nine peptides were determined: Thr-CySO3H, Pro-CySO3H, Asp-CySO3H, Phe-CySO3H, CySO3H-Glu, Tyr-[Asp, CySO3H], CySO3H-[Gly, Ser], Ser-[Asp, CySO3H], CySO3H-[Gly, Ser, Leu].
The authors wish to express their gratitude to Sankyo Co., Ltd. for their kind supply of ‘Takadiastase Sankyo’.View full abstractDownload PDF (301K) -
TANEAKI HIGASHI1960 Volume 47 Issue 3 Pages 326-334
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSRespiratory systems are greatly affected by the physiological conditions of the cell. Oxygen and nitrate as terminal electron acceptors of biological oxidation regulate the bacterial (Pseudomonas aeruginosa) respiratory chains, qualitatively and quantitatively. When the environmental conditions are altered, the concentration of each cytochrome component fluctuates according to its situation in the system. The oxygen respiration system, that is, the cyanide-sensitive and -insensitive, and nitrate-reducing systems were studied in this respect. Possible roles of P-cytochrome oxidase and P-hydroquinone oxidase in the terminal electron transport are discussed.
This work was supported in part by Grant-in-Aid for Fundamental Scientific Research from the Ministry of Education.
The author would like to express his thanks to Prof. K. Okunuki and Dr. T. Horio for their valuable guidance. Thanks are also due to his colleagues Messrs. M. Nozaki, T. Yamanaka, J. Yamashita and H. Mizushima of the same laboratory for their help and discussion and Messrs. M. Nakai, K. Yamazaki and K. Kusai of Amagasaki Factory of Nagase & Co., Ltd., for massculture of the bacteria.View full abstractDownload PDF (537K) -
I. A SEMI-MICRO GRADIENT ELUTION CHROMATOGRAPHY WITH DOWEX 1 FORMATE AND IDENTIFICATION OF SOME PHOS-PHATE ESTERS ON THE CHROMATOGRAMSHIGEO HORIE, SHIN-ICHI TERADA1960 Volume 47 Issue 3 Pages 335-350
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A modified semi-micro gradient elution chromatography for the analysis of tissue acid-soluble phosphorus compounds was described. One to 3g. of tissue could be analysed by this method.
2. Liver, muscle, and thymus tissue of rats were analysed and the chromatograms were illustrated.
3. The distribution and turnover of the acid-soluble phosphorus compounds in rat liver were also studied by P32 injection with the use of the semi-micro meteod.
4. Glucose-6-phosphate and L-α-glycerophosphate were identified on the chromatogram, and a phosphorus compound containing amino acid was separated from the Dowex l formate unadsorbable fraction.
The authors were greately indebted to Prof. N. Shimazono for his advice and encouragement. Thanks are due to Dr. M. Nakao, associate professor of the University of Gunma, for his kind gift of phosphate esters. The authors also wish to express their thanks to Mr. T. Kinoshita for his technical assistance in carrying out the paper chromatography.View full abstractDownload PDF (771K) -
I. ADAPTIVE FORMATION OF CYANIDE RESISTANT RESPIRATORY SYSTEM IN GROWING CELLSSHÔJI MIZUSHIMA, KEI ARIMA1960 Volume 47 Issue 3 Pages 351-360
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. One strain of Achromobacter isolated from soil was found to show a cyanide resistant growth adaptively in the presence of 10-3 M of cyanide.
2. The respiration of the cyanide adapted cells was cyanide insensitive, whereas that of the cyanide non-adapted cells was remarkably inhibited by cyanide.
3. The oxidation of DPNH and succinate by the cell-free preparations obtained from the cyanide non-adapted cells was remarkably inhibited by cyanide, whereas that obtained from the adapted cells was less inhibited.
4. The DPNH or succinate oxidase activity was almost located in the subcellular particulate fraction, and the terminal oxidase was found to be a one electron carrier.
5. Cytochromes b, a1, and a2 were found in the particulate fraction in both the cyanide adapted and the non-adapted cells. However, the amounts of cytochrome a2 (and a1) were greatly increased during the adaptation to cyanide.
6. It was postulated that the mechanism of cyanide resistance in the bacteria was caused by the increase of cytochrome a2 (or a1) which may be strongly inhibited by cyanide in nature. This is a new type of the mechanism in the drug resistance.
The authors wish to express their sincere appreciation to Dr. K. Sakaguchi for his kind guidance throughout this work. Thanks are also due to Mr. K. Komagata for his kind advice in the diagnosis of bacteria, to Mr. S. Miyazawa for the assay of riboflavine, and to Miss. M. Nakano for the isolation of the bacteria used.View full abstractDownload PDF (621K) -
III. THE INACTIVATING MECHANISM OF SULFHYDRYL ENZYMES BY γ-IRRADIATIONSHOZO TANAKA, HIROYUKI HATANO, SHIGETAKE GANNO1960 Volume 47 Issue 3 Pages 361-368
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Among the oxidizing agents produced by irradiation of γ-rays on water, OH and O2H radicals and hydrogen peroxide were proved to be effective to cause inactivation of the enzymes whose sulfhydryl groups are responsible for their activity. In the case of yeast ADH, it was shown that 46.5 per cent of the inactivation was caused by OH radical, 29.3 per cent by O2H radical and 24.2 per cent by hydrogen peroxide.
2. When cysteine in aqueous solution was irradiated by γ-rays the amount of sulfhydryl groups of cysteine molecule was found to decrease linearly with the dose of γ-rays.
3. It was demonstrated that the amounts of sulfhydryl groups in yeast ADH and liver GDH decreased with the increase of the doses of γ-irradia-tion. In the case of urease, the γ-irradiation caused a lowering of enzyme activity in proportion to the decrease in amount of the sulfhydryl groups.
4. The mechanism of inactivation of sulfhydryl enzymes caused by ionizing radiation as proposed by Barron was confirmed in the case of the inactivation of urease by relatively moderate doses of γ-rays.
The authors wish to express their thanks to Prof. T. Fukuda, Kyoto University, for his kind permission to use the Teletherapy Unit at the University Hospital of Kyoto.View full abstractDownload PDF (471K) -
I. PURIFICATION AND PHYSICOCHEMICAL PROPERTIES OF MULTIPLE COMPONENTS IN TURNIP PEROXIDASETOICHIRO HOSOYA1960 Volume 47 Issue 3 Pages 369-381
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. It was found by means of filter-paper electrophoresis that at least three kinds of peroxidases are present in the crude extract of turnip roots used in the present experiment.
2. These three peroxidases were isolated separately and highly purified, and designated as “turnip peroxidases A1, A2 and D” Turnip peroxidase D was obtained in a crystalline form (needle shape).
3. Physicochemical properties of these preparations were examined and thier homogeneity was confirmed. All these peroxidases obtained had the same prosthetic group as that of horseradish peroxidase, and their molecular weights or sedimentation coefficients were found almost same each other. They exhibited, however, different behaviour in electrophoresis.
4. The P. Z. of turnip peroxidase D was comparable to that of horseradish peroxidase II or that of Japanese-radish peroxidase a, while the P. Z. of turnip perosidases A1 and A2, in spite of the highest R. Z. of these enzymes, were considerably lower than that of turnip peroxidase D.
5. Besides the above peroxidases JP-A1 A2 and D), another peroxidase having the absorption spectrum similar to that of horseradish peroxidase I was obtained. However, this peroxidase was considered to be a substance produced during the course of isolation.
The author wishes to express his sincere thanks to Prof. B. Tamamushi, Dr. S. Nagakura and Y. Ogura of the University of Tokyo for their invaluable advice and encouragement throughout this work. He is indebted to Prof. N. Ui of Gunma University for the sedimentation measurements and to Dr. H. Nakamura of the Institute for Infectious Diseases, the University of Tokyo, for boundary electrophoresis measurements. Thanks are also due to Dr. I. Yamazaki of Tohoku University and Dr. Y. Morita of Kyoto University for their valuable suggestions for the preparation procedures. This study was aided in part by a Grant-in-Aid for the Scientific Research from the Ministry of Education given to the Research Group on the “Mechanism of Enzyme Action”.View full abstractDownload PDF (1973K) -
V. PROPERTIES OF COPPER IN PURIFIED CYTOCHROME ASHIGEKI TAKEMORI1960 Volume 47 Issue 3 Pages 382-390
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. It was found that a purified preparation of cytochrome a contains one atom of copper per one atom of iron or per mole of cytochrome a. Further, copper is presented at all of the stages of the purification in a quantity equal to at least one atom per mole of cytochrome a.
2. The cytochrome oxidase activity is inhibited by copper-ehelating agents such as ferrocyanide, salicylaldoxime and ethylxanthate.
3. The copper in cytochrome a is not released from the protein moiety by dialysis against copper-chelating agents. Acid treatment of cytochrome a easily releases the copper from the protein moiety. These observations show that the copper is firmly associated with cytochrome a.
4. It appears that the copper in cytochrome a exists in the cupric state, and that changes in the valency of the copper occur on electron transfer from substrate to oxygen.
The author is greatly indebted to Prof, K. Okunuki and Dr. I. Sekuzu for their kind advice, and would like to thank Messers. T. Yonetani, Y. Orii and K. Ohnishi for helpful discussion during the course of this work.View full abstractDownload PDF (538K) -
KATURA TUZIMURA, HIROSI MEGURO1960 Volume 47 Issue 3 Pages 391-397
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThree different cells of Rhizobium japonicum, viz. the cells grown on glucose, the cells grown on succinate, and the cells taken from soybean nodules, were compared in respect with the ability to oxidize substrates, including carbohydrates, the intermediates of glycolysis and the organic acids of Krebs, cycle.
Organic acids were readily oxidized by all the three types of the cells. Among the hexose and triose-phosphates, only fructose-1, 6-diphosphate was oxidized readily. Glucose was oxidized readily only by cells cultured on glucose, and slowly by the cells cultured on succinate, but not by the symbiotic cells. The symbiotic cells did not oxidize any of glucose, fructose, sucrose and mannitol. These facts suggest that the energy sources of Rhizobium in symbiotic state are organic acids but not carbohydrates, although it is. possible that fructose-l, 6-diphosphate is also used.View full abstractDownload PDF (439K) -
KENTARO TANAKA1960 Volume 47 Issue 3 Pages 398-399
Published: March 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (117K)
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