Bulletin of the Agricultural Chemical Society of Japan
Online ISSN : 1881-1272
Print ISSN : 0375-8397
ISSN-L : 0375-8397
Volume 24, Issue 4
Displaying 1-17 of 17 articles from this issue
  • Yukio SATOMURA, Susumu OI, Akira SAWADA, Juichiro FUKUMOTO
    1960 Volume 24 Issue 4 Pages 329-333
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The lipase and phospholipase of Sclerotinia Libertiana extracted from the cells with a dilute ammonium hydroxide solution could be fractionated by precipitation and adsorption-elution methods, and a partial purification of the lipase removed the activity towards Tween 20.
    From the examination of hemolysis and of phosphorus release from lecithin, the phospholipase was shown to involve types A, B and C. Phospholipase A was purified and obtained in crystalline form. The heat-stability of phospholipase A and C, and substrate specificity of the two lipases are also presented in this paper.
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  • Part I. On the Changes of Bindings of Actin to Alkaline Earth Metals during Aging of Meats
    Masao FUJIMAKI, Nobuhiko ARAKAWA, Hiroko YONETA
    1960 Volume 24 Issue 4 Pages 333-337
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The content of alkaline earth metals in actin during aging of meats was determined. The content in actin was found to be maximum immediately after slaughter and minimum at two days of aging. The rate of calcium to alkaline earth metals except calcium was high immediately after slaughter, but became low during aging.
    As the content of alkaline earth metals in actin extracted from the acetone dried actomyosin has been found to be less than that from the same muscle, the result obtained appears to show that in meats actin exists in both, free and bound form, the latter being one constituent of actomyosin, and at the process of aging in which minimum content of alkaline earth metals in actin was observed, actin was more in the form of actomyosin than at other process.
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  • Part II. Relation between Adsorption of Acid Antiseptics on Yeast Cell and their Toxic Effect
    Satoru OKA
    1960 Volume 24 Issue 4 Pages 338-343
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The acid antiseptics (salicylic, benzoic, dehydroacetic and sorbic acid) transferred to the yeast cell exist in two states, i.e., the adsorbed one on the solid phase of the cell and the dissolved one in the inner cell fluid.
    The adsorbed quantity of the antiseptics increases by the addition of inorganic salts in the medium. The toxic effect on the yeast also increases with the increase of the salts concentration, being independent of the biological effect of the salts themselves. On the other hand, the dissolved quantity changes with the content of inner cell water which can be controlled by the physical action of the osmotic pressure in the medium. However, the toxic effect is independent of the change of the dissolved quantity.
    As the conclusion, it is considered that the adsorbed quantity is the limiting factor of the toxic effect.
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  • Kenji MORI, Michinori NAKAMURA, Saburo FUNAHASHI
    1960 Volume 24 Issue 4 Pages 344-350
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Phosphate compounds in potato tubers were fractionated by ion-exchange chromatography. By the use of radio-phosphorus, the following compounds were tentatively identified to be present in potato tubers: G-1-P, G-6-P, F-6-P, FDP, PGA, AMP, UMP, ADP, UDPX, UDPG and ATP. When the tubers were stored at a low temperature, the contents of organic phosphate compounds showed u considerable increase over those of potatoes stored at 4 high temperature. However, the relative composition of each component was not much influenced by the storage temperature except ATP which showed a great increase at a lower temperature.
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  • Part XII. Occurrence of Glyoxylic Acid Reductase
    Hideo KATAGIRI, Tatsurokuro TOCHIKURA
    1960 Volume 24 Issue 4 Pages 351-356
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Isocitritase was found in Achromobacter superficialis, Zygosaccharomyces soya and major in addition to coli-aerogenes. The mode of degradation of citrate was investigated with both the cell-free extracts and the ammonium sulfate-precipitates of coli-aerogenes. The addition of TPN** to the reaction mixtures brought about a striking increase in the yield of α-ketoglutarate against the decreasing yield of glyoxylate.
    Little or no formation of α-ketoglutarate occurred when incubations were carried out with citrate in the presence of a large amount of succinate. However, when glyoxylate was added to a citrate-containing medium, the anaerobic formation of α-ketoglutarate took place even under such conditions as in the presence of succinate. Glyoxylate was found to be reduced to glycollate by the bacterial preparations. Pseudomonas fluorescens was also observed to produce glycollate from citrate. It was demonstrated that the formation of α-ketoglutarate with citrate is the result of a coupling reaction between isocitric dehydrogenase and glyoxylic reductase.
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  • Part XIII. The Enzymic Oxidation of Glycollic Acid to Glyoxylic Acid
    Hideo KATAGIRI, Tatsurokuro TOCHIKURA
    1960 Volume 24 Issue 4 Pages 357-361
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The oxidation of glycollate to glyoxylate by molecular oxygen was found to be catalyzed by the dried cells of coli-aerogenes bacteria such as E. coli and A. aerogenes, and baker's yeast. The enzyme (glycollic oxidase) was ascertained to be contained in the bacterial cells of coli-aerogenes grown aerobically on various media such as glucose-ammonium salt, acetate-bouillon and citrate-bouillon. The bacterial cells with citritase and isocitritase were also found to contain glycollic acid oxidase. The cell-free extracts of coli-aerogenes were fractionated with ammonium sulfate for glycollic acid oxidase. The enzyme was resolved to yield an inactive apoenzyme which could be reactivated by the addition of FMN** or FAD. The enzyme was found to be strongly inhibited by cyanide. It was suggested that a glyoxylate_??_glycollate system may function in the respiration of microorganisms.
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  • Part IV. The Quinary System KCl-K2SO4-MgCl2-MgSO4-Mg(OH)2-H2O at 50°
    Michio NAKAYAMA
    1960 Volume 24 Issue 4 Pages 362-371
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The quinary system KCl-K2SO4-MgCl2-MgSO4 Mg(OH)2-H2O and associated eight systems K2SO4-MgSO4 Mg(OH)2-H2O, MgCl2-MgSO4-Mg(OH)2-H2O, KCl-MgCl2 Mg(OH)2-H2O, KCl-K2SO4 Mg(OH)2-H2O, MgSO4-Mg(OH)2-H2O, MgCl2-Mg(OH)2-H2O, K2SO4-Mg(OH)2-H2O and KCl-Mg(OH)2-H2O were investigated at 50° The solid phases of these systems were the new basic triple salt (NS salt B), MgCl2•3Mg(OH)2•8H2O, MgSO4•5Mg(OH)2•3H2O, carnallite, leonite, kieserite, hexahydrite, bischofite, potassium chloride, potassium sulfate and magnesium hydroxide and the crystallization fields of these salts in nine systems were determined.
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  • Part I. Isolation and Characterization of Several Physiologically Active Neutral Substances
    Yu-Shih CHEN
    1960 Volume 24 Issue 4 Pages 372-381
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Three kinds of diketopiperazines which have retarditive activity for the growth of plant seedlings and plant roots at concentrations ranging from 1:2, 500 to 1:100, 000, were isolated from the neutral fraction by extracting the cultured broth of Rosellinia necatrix. These three diketopiperazines have been proved to be L-prolyl-L-leucine anhydride, L-prolyl-L-valine anhydride and L-prolyl-L-phenylalanine anhydride respectively, and the last one seems to be a new diketo-piperazine.
    Furthermore, a crystalline wax having m.p. 52°C, a physiologically inactive substance, was also isolated from the same neutral fraction and presumed to be the saturated hydrocarbon of n-pentacosane C25H52.
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  • Part III. The Decompositions of Several Cysteine-aldehyde Compounds in Aqueous Solutions
    Junya MIZUTANI, Yataro OBATA, Yoshinori ISHIKAWA
    1960 Volume 24 Issue 4 Pages 382-385
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Cysteine-aldehyde compounds were prepared by the reactions of L-cysteine with formaldehyde, acetaldehyde, n-butyraldehyde, benzaldehyde and furfural in 50% ethanol solutions. Hydrogen sulfide and ammonia liberated from cysteine-aldehyde compounds in heated aqueous solutions (oil bath: 120°C) were determined. Although thiazolidine derivatives were stable generally in boiling aqueous solution, L-cysteine-furfural compound was unstable and a large amount of hydrogen sulfide compared with other compounds was released.
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  • Part X. Influence of the Environmental Factors on the Change of Microflora during the Ripening Process of Soy-mash
    Hiroshi ÔNISHI
    1960 Volume 24 Issue 4 Pages 386-396
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Influences of concentrations of sodium chloride and pH values of soy mash on the changes of microflora during the ripening process were investigated. The proportions of various yeasts in the soy mash were proved to be changed with the above two. environmental factors. And it was shown that growth sequence of yeasts in soy mash was controlled according to their pH sensitivities at the hypertonic condition. From young soy mash (3 days' old), the following yeasts were isolated: salt-tolerant type……Saccharomyces rouxii Boutroux, Torulopsis famata (Harrison) Lodder et Kregervan Rij, Candida polymorpha Ohara et Nonornura, Pichia farinosa (Lindner) Hansen, and Trichosporon behrendii Lodder et Kreger-van Rij; salt-sensitive type……Candida tropicalis (de Beurm., Gougerot et Vaucher) Ota and Candida rugosa (Anderson) Diddens et Lodder.
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  • Part IX. The Direct and Indirect Formation of the Silkprotein during the Growth of the Silkworm Larva
    Toshifumi FUKUDA
    1960 Volume 24 Issue 4 Pages 396-401
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1) The present study was carried out to clarify a mechanism of the formation of the silkprotein during the growth of the silkworm larva.
    2) A large part, about 70 per cent of the silkproteins produced by one silkworm is directly derived from the proteins of the mulberry leaves (direct formation), but some part of the silkproteins, about 30 per cent, is also derived from the tissue proteins and body fluid proteins, in relation to the metamorphosis of the silkworm larva (indirect formation); there are two pathways in the formation of the silkproteins during the growth of the silkworm larva, i.e., direct formation and indirect formation.
    3) The direct formation of the silkproteins takes place, in the hybrids of Japanese race and Chinese race, during the period between the 4th day of the 5th instar and maturity, but the indirect formation takes place during the period from the 8th day of the 5th instar to just before termination of spinning after reaching maturity. My thanks are due to Mr. Mitsumasa Suto, Mr. Motoichi Matuda, Mr. Tsutomu Kurose and Mr. Yoshiaki Horiuchi for their skilful technical assistance in the current work,
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  • Part V. Syntheses of (-)-Isopulegol and (+)-Neo-isopulegol
    Hiroo UEDA, Sumio SHIMIZU
    1960 Volume 24 Issue 4 Pages 402-404
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    (-)-Isopulegol and (+)-neo-isopulegol were isolated by a partial esterification of isopulegol mixture, obtained by the hydrolysis of the condensation product of (+)-citronellal with acetic anhydride. From the infrared spectra and optical rotation, it has been shown that isopulegol synthesized from (+)-citronellal mainly consists of (-)-isopulegol and (+)-neo-isopulegol in approximately equal amounts, but the presence of other isomers is negligible.
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  • Isao KANAI
    1960 Volume 24 Issue 4 Pages 405-412
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Effects of physical and chemical properties on whiteness of cigarette ash have been studied. The whiteness of cigarette ash could be measured successively with a Photovolt Photoelectric Reflection Meter. In cigarettes made from Bright leaves, the reflectance has close relationships with weight per cigarette and the smoking conditions such as puff volume and frequency of puff; on the contrary, in cigarettes made from Burley or Japanese Native leaves, the reflectance is almost constant under any weight per a cigarette and any smoking conditions. The whiteness of cigarette ash of various tobacco leaves decreases in the following order: Bright (and Turkish), Japanese Native “Matsukawa-ha”, Burley, and Japanese Native “Daruma-ha”- Both the kinds and amounts of each inorganic constituent contained in the leaves vary the whiteness of cigarette ash.
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  • Part III. Adsorption of Esters of p-Hydroxybenzoic Acid on Yeast Cell and their Toxic Effect
    Satoru OKA
    1960 Volume 24 Issue 4 Pages 412-417
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Alkyl esters of p-hydroxybenzoic acid rapidly transfer from the medium to the yeast cell, and the transferred ester is accumulated in the cell. The transfer ratio of the ester increases as the alkyl radical becomes higher, and also, its toxic effect on the yeast increases in the same manner.
    In this case, a part of the transferred ester is adsorbed on the solid phase of the cell and the other part is dissolved in the lipid phase and in the inner cell fluid. When the alkyl radical of the ester is changed, it is observed that a definite quantity of the adsorbed ester is required in order to give a definite inhibiting effect on the yeast growth, though the concentration of the dissolved ester in the lipid phase and in the inner cell fluid changes. Accordingly, it is concluded that the toxic effect mainly depends upon the adsorbed esters, being independent of the dissolved ester in the lipid phase or in the inner cell fluid.
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  • III. Mechanism of Substrate Inhibition
    Hideo CHIBA, Etsuro SUGIMOTO, Makoto KITO
    1960 Volume 24 Issue 4 Pages 418-423
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The mechanism of the substrate inhibition in the yeast PGA mutase reaction has been studied in detail.
    It is concluded that the case of (a) or (c) is suitable to the mode of this substrate inhibition.
    It is confirmed that the coenzyme competes with the substrate for the coenzymebinding site on the enzyme; the substrate is a competitive inhibitor of the coenzyme.
    The Michaelis constant for the coenzyme (Kc) is calculated to be 1.3×10-5 M or less than that.
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  • IV. Mechanism of Some Inhibitiones
    Hideo CHIBA, Etsuro SUGIMOTO, Makoto KITO
    1960 Volume 24 Issue 4 Pages 424-427
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    In yeast PGA mutase reaction, the inhibition by Zn++ is competitive for the coenzyme.
    Pyrophosphate also acts as a competitive inhibitor of the coenzyme.
    It is found that the enzyme is protected by EDTA from the fluoride inhibition when EDTA is added into the reaction mixture before the enzyme is preincubated with the substrate and fluoride.
    It seems that fluoride, irreversibly forms an inactive complex with the enzyme in the presence of the substrate.
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  • V. Separation and Crystallization of Each Component from Crystalline Phosphoglyceric Acid Mutase
    Hideo CHIBA, Etsuro SUGIMOTO, Makoto KITO
    1960 Volume 24 Issue 4 Pages 428-433
    Published: 1960
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Boundary electrophoretic behaviors of crystalline yeast PGA mutase have been studied in veronal and phosphate buffers. The crystalline enzyme used here is composed of five components.
    Each component has been separated in a large quantity by using the special vertical zone electrophoresis apparatus with Hg-Hg2Cl2 reversible electrodes, which is deviced to compensate electroosmotic flow automatically.
    The components I to IV are the PGA mutase protein and have different specific activities.
    Each separated component has been crystallized by the dropwise addition of saturated ammonium sulfate solution.
    The crystalline form of each component separated is the same as the original one.
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