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Volume 46 (1959)
- Issue 6 Pages 669-
- Issue 5 Pages 535-
- Issue 4 Pages 397-
- Issue 3 Pages 219-
- Issue 2 Pages 107-
- Issue 1 Pages 1-
Volume 46, Issue 5
Displaying 1-13 of 13 articles from this issue
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TAMITARO MIZUNOYA1959 Volume 46 Issue 5 Pages 535-547
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThis paper considers some aspects of the stationary state of the me-tabolizing system which has such a cyclic pathway as the TCA cycle. In Part I, first of all, an equation for the rate of dissipation of the available energy in the metabolizing system is derived, in general, from the view-point of the “thermodynamics of irreversible processes”. Secondly this equation is applied to the system with a reaction of catalytic cycle and it is shown that the stationary state appears only under the situation of the conservation of the amount of cycle components. In Part II, a special case is kinetically treated in which any branch reaction which is able to vary the amount of the catalyst or cycle components themselves does not occur, and it is shown that the reaction rate of each step in the cyclic process becomes equal with one another as the time goes to infinity; in other words, the stationary vortex appears among the cycle components. Subsequently, the energy dissipation To0 in the stationary vortex of the cyclic catalyst is formulated as
To0=[C0]X/τ,
where [C0] is the total concentration of the catalyst or cycle components, X is the chemical affinity of the overall reaction catalyzed by the cyclic process and τ is the period of a revolution of the cycle. This equation can be alternatively derived from an approximate equation of the energy dissipation. Finally, it is suggested from this equation that the catalytic systems with cyclic processes have been probably developed towards the direction of a longer period of the cycle and the metabolic patters have been perhaps complicated by the addition of new reaction steps in the cyclic processes.
The author wishes to express his hearty thanks to Prof. K. Oomori and Ass. Prof. G. Tomita of this laboratory for their advice and encouragement, and to Prof. S. Akabori of Osaka University for encouragement and interest in his work. The authr's thanks are especially due to Prof. M. Sugita of Hitotsubashi University for his valuable advice and continual encouragement and to Prof. K. Watanabe of this university for his kind advice in preparation of the manuscript.View full abstractDownload PDF (543K) -
VI. ELECTROPHORETIC STUDY OF THE INTERACTION OF β-LIPOVITELLIN WITH POLYANIONSHIROSHI SUGANO1959 Volume 46 Issue 5 Pages 549-557
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Electrophoreses on the mixtures of β-lipovitellin and a series of polyanions (RNA, heparin, and alginic acid) have represented the reversible formation of soluble complexes between the components.
2. The influences of pH and ionic strength to the interaction have shown that not only the electrostatic forces but also the van der Waals forces contribute to stabilize the interaction.
3. The affinities of three polyanions to β-lipovitellin have been compared by their mean equivalent weights.
4. From the electrophoretic patterns, it has been concluded that the polyanions form the complex with β-lipovitellin without splitting off the lipid-protein bond.
5. An attempt of quantitative interpretation of the interaction has been made.
The author wishes to express his sincere thanks to Prof. N. Ui of Gumma University for his valuable suggestions.View full abstractDownload PDF (390K) -
HISASHI NAKAJIMA1959 Volume 46 Issue 5 Pages 559-570
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Monoamine oxidase from the liver and brain was inhibited by chlorpromazine. This inhibition was not reversed by cysteine, glutathione or FAD.
2. Monoamine oxidase was inhibited in decreasing order by chlorproma-zinc, phenergan, promazine, dichlorpromazine, 3-chloro, 10-piperidinoacetyl phenothiazine and chlorpromazine sulfoxide. Lysergic acid diethylamide stimulated MO slightly.
3. Chlorpromazine had no effect liver MO in vivo, while it slightly decreased 5-hydroxyindole acetaldehyde formation from serotonin by brain MO.
4. Several metabolites of serotonin were found in vitro in homogenates of various organs. One of these seemed to be N-methylserotonin.View full abstractDownload PDF (451K) -
YOSHITO HARA1959 Volume 46 Issue 5 Pages 571-573
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA method of ion exchange separation of sugar phosphates including F-1-P was described. The sugar phosphate in each fraction was identified by paper chromatography. The recovery of each sugar phosphates was 90 to 95 per cent.View full abstractDownload PDF (109K) -
SUEO TATSUOKA, AKIRA MIYAKE, SHYOZO WADA, ISUKE IMADA, CHIKASHI MATSUM ...1959 Volume 46 Issue 5 Pages 575-581
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSR-302, a strain belonging to Rhizopus, was cultivated aerobically and from the filtered broth, partially purified lipase was obtained by fractionation with ammonium sulfate and subsequent adsorption by calcium phosphate. A solution of the product was poured through a column of a 1:3 mixture of calcium phosphate and Celite, and then eluted with 0.2, 0.4, 0.8, 1.5, 3.0 and 12 per cent ammonium sulfate solutions, successively. Two protein portions having the activity of lipase were eluted by the 1.5 and 3 per cent ammonium sulfate solutions respectively, and the former was named α-lipase and the latter β-lipase. These lipases are extremely unstable as solution in water but are a little stabilized in the presence of salt. Their aqueous solutions lose activity by half in one hour at 30-40° and become completely inactive in one hour at 60°, and also at pH higher than 8.5. The partially purified lipase has two pH optima at 4.9 and 6.8 and the former corresponds with the pH optimum of α-lipase and the latter with that of β-lipase. Paper electrophoresis of the partially purified lipase gives two spots, one of which migrates fast and the other slowly, and their speeds correspond with those of α- and β-lipase, respectively.
The authors are grateful to Dr. S. K u wad a and Dr. K. Sato for their encourage-ment throughout this work. Thanks are also due to members who performed tank culture.View full abstractDownload PDF (288K) -
AKIRA TSUGITA1959 Volume 46 Issue 5 Pages 583-592
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTAA was dinitrophenylated and partly hydrolysed with 85 per cent formic acid. The N-terminal DNP-peptides were extracted from the hydro-lysate and separated from each others by means of countercurrent distribution method and other kinds of techniques. The purified DNP-peptides were then analysed for amino acid compositions, N- and C- terminal residues, etc. From these analytical experiments, it was concluded that the amino acid sequence in the N-terminal region of TAA is alanyl-glycyl-aspartyl-glutamyl-seryl-alanyl-leucyl-threonine.
The author wishes to express his gratitude to Prof. S. Akabori for his kind guidance, and to Dr. T. Ikenaka for his helpful advice during the course of this investigation, and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.View full abstractDownload PDF (423K) -
AKIHIKO KAJITA, FUJIKO UCHIMURA, HITOSHI MIZUTANI, GORO KIKUCHI, KOOZO ...1959 Volume 46 Issue 5 Pages 593-605
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Dissociation of histidine hemichrome coincided well with a theoretical second order dissociation curve. The change of pK in function of pH was elucidated by taking into consideration the dissociations of imidazole-NH of histidine and of hematin iron. The following theoretical equation was found to account for the results obtained.
pK=pKo-2log(1+[H+]/Ka)-log (1+Kb/[H+])
pK0 was found to be 3.6 on an average, at room temperature of 20°. 2. Alkaline denatured proteins combined with much more heme molecules than expected from their histidine contents. The number of heme linked groups was estimated as 68, 26, 40 and 32 in horse hemoglobin, bovine serum albumin, horse serum albumin and human serum γ-globulin, respectively. The heme linked groups of alkaline denatured proteins were deduced to be not carboxyl groups of acidic amino acids but nitrogenous groups of basic amino acids.
3. The affinity of alkaline denatured protein towards heme was decreased remarkably by proteinase digestion.
The authors wish to express their gratitude to Miss M. Shinoda for her technical assistance, to Dr. H. Hirai for the gift of horse serum albumin and human serum γ-globulin, and to Dr. T. Kusunoki for the sample of bovine serum albumin. Thanks are also due to the Scientific Research Fund of the Ministry of Education for grant. The essential part of this study was published in Japanese elsewhere (15, 16).View full abstractDownload PDF (475K) -
II. ON THE CHEMICAL STRUCTURE OF OLIGOMANNOINOSITIDESSHOSHICHI NOJIMA1959 Volume 46 Issue 5 Pages 607-620
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe chemical structure of oligomannoinositides isolated from Wax D of BCG was proposed and discussed. Barium salts of glycerophosphorylinositoldi-, tetra- and penta-mannosides were isolated in pure states from oligoman-noinositides. Fatty acids of oligomannoinositides were proved to be composed of palmitic acid and an acid having the neutral value of 188.
The author is very grateful to Dr. D. Mizuno, Chief of the Department of Chemistry, National Institute of I-lealth, Tokyo, for his constant encouragement and kind guidance throughout experiments of this work. He also expresses his thanks to Prof. Dr. T. Ukita, of the Faculty of Pharmaceutical Sciences, University of Tokyo, for his constant encouragement and helpful suggestions during the course of this work. Thanks are also due to Miss E. Kondo of the Department of Chemistry, National Institute of Health, Tokyo, for her skillful technical assistance in every experiment of this work. Microanalyses for carbon and hydrogen were carried out by Miss S. Hara of the Department of Chemistry, National Institute of Health, Tokyo.View full abstractDownload PDF (883K) -
III. ACCUMULATION OF α-KETO ACIDS IN BIOTIN-DEFICIENT CULTURE OF PIRICULARIA ORYZAEHIROHIKO KATSUKI1959 Volume 46 Issue 5 Pages 621-627
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Piricularia oryzae accumulates pyruvic, α-ketoglutaric and dimethyl-pyruvic acid in the biotin-deficient culture. In the thiamine-deficient culture, it accumulates pyruvic and α-ketoglutaric acid, but does not accumulate dimethylpyruvic acid.
2. Biotin-deficiency scarcely has effect upon the biosynthesis of CoA from dimethylpyruvic acid in this organism.
3. The contents of ATP and pyridine nucleotides were found to be remarkably decreased in the biotin-deficient mycelia. Correspondingly the amount of unstable phosphate compounds was also observed to decrease under this condition.
The author is indebted to Prof. Shozo Tanaka, Kyoto University, for his helpful criticism and encouragement during the course of this work.View full abstractDownload PDF (292K) -
SAKAE KATOH1959 Volume 46 Issue 5 Pages 629-632
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (171K) -
AKIHIKO HATTORI, YOSHIHIKO FUJITA1959 Volume 46 Issue 5 Pages 633-644
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFrom the cells of a fresh-water blue-green alga, Tolypothrix tenuis, the three components of phycobilin pigments (phycocyanin, phycoerythrin and allophycocyanin) were isolated and purified to crystalline states by combined use of salting-out method (using ammonium sulfate) and adsorption method (using tricalcium phosphate-gel) followed by the technique of ultracen-trifugation.
Using the highly purified samples, determinations were made of the various physicochemical properties of the chromoproteids, including the sedimentation and diffusion constants, electrophoretic mobilities, isoelectric points, molecular weight and elementary composition, and the results obtained were compared with those reported earlier by other workers.
The authors wish to express their gratitude to Profs. H. Tamiya, A. Takamiya and A. Watanabe, University of Tokyo, for their valuable advices during this work. Thanks are also due to Drs. T. Takeda and T. Samejima, Tokyo Institute of Technology, and Dr. K. Nagai, Institute of Infectious Diseases, University of Tokyo, who helped the writers in carrying out the measurement of sedimentation constants.View full abstractDownload PDF (808K) -
I. ACTION OF TRYPSIN ON MONO-, DI-, TRI- AND TETRA-GLYCYL-L-LYSINAMIDENOBUO IZUMIYA, HAKARU UCHIO1959 Volume 46 Issue 5 Pages 645-652
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A number of (glycyl)n-L-lysinamide dihydrochlorides in which n are 1, 2, 3 and 4 have been synthesized and tested as substrates for trypsin.
2. By the use of glycyl-L-lysinamide, the pH optimum of hydrolysis was found to be near 8.2. For comparison, the pH optimum for benzoyl-L-argininamide was checked and found to he near 7.8.
3. The values of proteolytic coefficients at the initial substrate concen-trations of 0.025 M, 0.015M, 0.0M, and 0.005M, d Cmax, determined at 30° and pH 8.0, were taken as measures of the relative susceptibility of hydrolysis of the substrates by trypsin. It was determined that the order of susceptibility to hydrolysis is listed as: diglycyl≥triglycyl->tetraglycyl-> monoglycyl-L-lysinamide.
4. Chromatographic analysis of the reaction mixture proved the simple hydrolysis of the substrates to the corresponding (glycyl)n-L-lysine and NH3.
The authors wish to thank Prof. S. Shibuya for his interest, and Dr. A. Tanaka for his discussion in this study. The authors also thank Dr. J. P. Grcenstcin, Dr. M Winitz and Dr. S. M. Birnbaum for generous gift of the amino acids and the enzyme.View full abstractDownload PDF (292K) -
I. PURIFICATION OF A PROTEASE OF STREPTOMYCES GRISEUSMASAO NOMOTO, YOSHIKO NARAHASHI1959 Volume 46 Issue 5 Pages 653-667
Published: May 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. It was found by the authors that Streptomyces griseus, a typical strain used for the industrial production of streptomycin, produced a remarkable amount of protease in usual culture broth together with streptomycin.
This enzyme was separated from streptomycin and highly purified by a convenient method as follows: A filtrate of the broth was mixed with Na2HPO4 and CaCl2 and the resulting calcium phosphate gel was removed together with turbid impurities. From this clear solution, the enzyme was precipitated by salting out leaving streptomycin in the supernatant. After dissolving and dialyzing this enzyme precipitate, the resulting enzyme solu-tion was passed through a column of Kaken C-1 (SP-3) resin buffered at neutral pH and then the adsorbed enzyme was eluted with alkaline buffer solution containing high concentration of salts. From this eluate, the enzyme was concentrated and purified by salting out and acetone precipitation, and crystallized as needles from acetone solution.
2. In resin column treatment, a few of other kinds of resins such as Duolite C-10, S-30 or Kaken Phenol-type resin was also proved to be useful. On the basis of this experiment, the mechanism of adsorption between resin and enzyme was discussed.
3. It was proved by paper electrophoresis that the crystalline prepara-tion of this enzyme was composed of a single electrophoretic component. This enzyme was fairly stable over the pH range from 5 to 9, and its maximal activity was appeared at pH 7-8.
The authors wish to express their thanks to Dr. T. A kahira, Dr. M. Yanagita, Prof. K. Sakaguchi, Prof. K. Okunuki and Dr. B. Hagihara for their kind guidances and useful suggestions. The authors are also grateful to Mr. S. Fujita for preparation of the enzyme and to Mr. H. Kawabe for resins, besides their helpful advices during the course of this work. Thanks are also due to the Kaken Chemical Co., Ltd. for the continual supply of culture broth.
The present work was aided in part by the grant of Scientific Research Fund of the Ministry of Education for which the authors wish to thank.View full abstractDownload PDF (1101K)
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