Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Volume 28, Issue 12
Displaying 1-17 of 17 articles from this issue
  • Part VII. Degradation of Glycol Chitin and Chitin by the Chitinase System of Aspergillus niger
    Akira ÔTAKARA
    1964 Volume 28 Issue 12 Pages 811-818
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    The mode of degradation of glycol chitin and chitin by two enzyme fractions separated from Aspergillus niger was investigated. One of the enzyme rapidly cleaved the endo-β-glucosaminidic bonds in the polysaccharide chain, forming chitodextrin and oligosac-charides, while the other produced monosaccharide as a main product in the degradation. The successive action of the two enzymes was also examined. Intermediate products in the enzymatic degradation were surveyed using paper and column chromatography. Also, the over-all pattern of degradation of glycol chitin and chitin by the chitinase system of Aspergillus niger was discussed.
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  • Part II. Chemical Structure of the Product on Glucose and Gluconate Oxidation
    Yoshiharu WAKISAKA
    1964 Volume 28 Issue 12 Pages 819-827
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    On shaking culture of the newly isolated bacterium, Pseutdomonas albosesamae, 7) on glucose- or gluconate-containing medium, “a reducing acid” was produced in high yield. The product is produced specifically from glucose, gluconate and 2-ketogluconate, and not from other sugars. The product was isolated as a white to cream-colored, unstable, friable powder of calcium, barium or potassium satl by use of methanol precipitation technique.
    On manometric studies of glucose, gluconate and 2-ketogluconate oxidation by lyophilized cells, 1.38, 0.99 and 0.48 equimolar consumption of oxygen were observed, respectively, and a common product was detected in the reaction mixture by paper chromatography. Periodate oxidation of “a reducing acid” gives the formation of oxalic and glycolic acid as oxidation products. Hardly any formaton of formaldehyde was observed. Ruff's oxidation of the reduced fermentation product, prepared by sodium borohydrate or catalytic reduction using platinum oxide as catalyst, gave the formation of D-arabinose and lesser amounts of L-xylose. On catalytic reduction by Raney nickel as the catalyst, 2-ketogluconate was formed as the main product. 2-ketogulonic acid was detected paper chromatographically, but the identification was unsuccessful.
    The 2, 4-dinitrophenylhydrazone, analytically pure bis-2, 4-dinitrophenylhydrazone of diketogluconate, m. p. 156_??_157°C, [α]24.5D+57.2°, pyridine, 1 dm., was obtained as yellow needle crystals.
    From the above results, “a reducing acid” was certified to be 2, 5-diketogluconic acid.
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  • Part V. Acceptor Specificity of Nucleoside Phosphotransferase (I): Phosphorylation of Ribonucleosides
    Koji MITSUGI, Akira KAMIMURA, Eiji NAKAZAWA, Shinji OKUMURA
    1964 Volume 28 Issue 12 Pages 828-837
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1) Various kinds of naturally occurring ribonucleosides were found to be phosphory-lated by bacterial nucleoside phosphotrans-ferases using p-NPP as a phosphate donor at pH 4.0.
    2) Nucleotide-isomers synthesized are not always the same, but some bacteria belonging to genera Pseudomonas, Flavobacterium, Serratia and Staphylococcus were characterized to synthesize mainly 5'-isomer, whereas the others belonging to genera Aeromonas, Escherichia, Aerobacter and Proteus to phosphorylate preferably at C3', and C2', without distinction of purine or pyrimidine ribonu-cleosides.
    3) The ratio of 3' and 2'-isomer synthesized by the latter group of bacteria may be observed to be different; 3'-isomer seems to be preferentially synhtesized in the case of purine ribonucleoside, while 3'-isomer seems to be less than 2'-isomer in the synthesis of pyrimidine ribonucleotides.
    4) The cause of difference present between the synthesis of 2' and 3'-isomer by the latter group was discussed.
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  • Part VI. Acceptor Specificity of Nucleoside Phosphotransferase (II): Phosphorylation of Deoxyribonucleosides
    Koji MITSUGI, Eiji NAKAZAWA, Shinji OKUMURA
    1964 Volume 28 Issue 12 Pages 838-848
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1) Various kinds of deoxyribonucleosides were phosphorylated regardless of the replacement of acceptor ribonucleosides to deoxyribonucleosides.
    2) The main product isomer was observed to be invariable without distinction of riboand deoxyribonucleosides, but the bacteria characterized to phosphorylate at C5' of ribonucleoside produced 5'-isomer together with a little amount of 3'-isomer and “deoxyribo-nucleoside-X”, while the others characterized to synthesize 3'- and 2'-isomer phosphorylated only at C3'.
    3) The great difference present between the synthesis of ribonucleotides and deoxy ribonucleotides was on the synthesis of “de oxyribonucleoside-X”, probably deoxynucleo side-5', 3'-diphosphate, which was synthesizes from deoxyribonucleosides by only the bacteria of the former group.
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  • Part VII. Acceptor Specificity of Nucleoside Phosphotransferase (III): Phosphorylation of Unusual Ribonucleosides and Their Ribosyl Derivatives
    Koji MITSUGI, Akira KAMIMURA, Shingi OKUMURA, Noboru KATSUYA
    1964 Volume 28 Issue 12 Pages 849-858
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1) Various kinds of unusual ribonucleosides including 5- or 6-substituted pyrimidine and 2- or 6-substituted purine were phosphorylated by the cell-free extracts of typical strains of both groups, using p-NPP as donor.
    2) The bacteria characterized to synthesize 5'-isomer in the phosphorylation of naturally occurring ribonucleosides were observed to transfer the phosphoryl radical to 5'-CH2OH, while the others were observed to phosphorylate at C3' or C2', even if C5', is substituted by any radical.
    3) Although the specificities of these nucleoside phosphotransferases were confirmed to be valid, regardless of the structure of unusual ribonucleosides or their derivatives, some steric effects on these reactions may be considered, just as observed in the failure of OR phosphorylation by the latter group of bacteria.
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  • Part VIII. Acceptor Specificity of Nucleoside Phosphotransferase (IV): Phosphorylation of Adenylic Acid
    Koji MITSUGI, Eiji NAKAZAWA, Masahiro TAKAHASHI, Hideaki YAMADA
    1964 Volume 28 Issue 12 Pages 859-868
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1) Adenosine-5', 2'-diphosphate was found to be synthesized by incubating 2'-AMP with p-nitrophenylphosphate and a nucleoside phosphotransferase present in bacteria capable of phosphorylating at C5', but was not synthesized from 3'-AMP.
    2) Isomeric derivative, adenosine-5', 3' (or 2')-diphosphate, was also synthesized from 5'-AMP and the same phosphate donor by incubating with the nucleoside phosphotransferase present in bacteria which had been characterized to phosphorylate at C3' or C2'.
    3) These findings strongly indicate that specific correlation was observed among the structure of acceptor, the nucleotide-isomer synthesized and the grouping of bacteria capable of phosphorylating nucleosides already proposed.
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  • Part III. The Specificity of the Crystalline Acid-Protease on Synthetic Substrates
    Jiro SAWADA
    1964 Volume 28 Issue 12 Pages 869-875
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    1. Carbobenzoxy-L-glutamyl-L-tyrosine and benzoyl-L-argininamide are readily hydrolyzed by the acid-protease of Paecilomyces varioti Bainier TPR-220, as acid-proteases of Aspergillus oryzae by Nunokawa and Asp. saitoi by Yoshida did. But the present enzyme can not hydrolyze alanylglycylglycine and leucylglycylglycine which are hydrolyzed by the above two enzymes.
    2. The enzyme is optimally active at pH 3.5 and 5.5 toward carbobenzoxy-L-glutamyl-L-tyrosine and benzoyl-L-argininamide at 45°C respectively. These values of optimum pH, however, are different from that obtained from Asp. saitoi protease.
    3. The hydrolysis velocity constant, Michaelis constant, and activation energy in the hydrolysis of both substrates by the enzyme were determined.
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  • Part I. Isolation of a Producing Stratin Utilizing Blackstrap Molasses and the Effects of Incubation Temperature
    Koichi YAMADA, Hidemasa HIDAKA
    1964 Volume 28 Issue 12 Pages 876-883
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Isolation and screening tests were carried out in order to find microorganisms which were able to produce citric acid directly from blackstrap molasses. Some strains were obtained which accumulate considerable quantities of citric acid. Certain temperature changes during the course of incubation were found to increase the yield of citric acid.
    The present investigation was undertaken to see if a simple method could be found to improve the yield of citric acid from blackstrap molasses, and we could obtain the yield of more than 70% from the untreated molasses using a newly isolated strain of Asp. niger.
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  • Part I. Purification and Some Properties
    Kiyoshi MIZUSAWA, Eiji ICHISHIMA, Fumihiko YOSHIDA
    1964 Volume 28 Issue 12 Pages 884-895
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
    Proteolytic enzymes derived from thermophilic streptomyces sp. strain 1689 were purified and some properties were studied. A 8-fold purification was obtained from the culture supernatant by ammonium sulfate fractionation, acetone precipitation, and chromatography on CM-Sephadex. Two proteinases of almost identical properties were fractionated on CM-Sephadex chromatography. The purified preparations appeared to be homogeneous on ultracentrifugation. The optimum pH for proteolytic activity on casein was found to be pH 10.6_??_10.8. The stability was considerably increased by the addition of Ca++, and the proteinases exhibited a relatively high thermal stability. Enzyme activity was inhibited by oxidizing agents, PCMB, potato inhibitor, DFP, and heavy metal ions. Na+, K+, Mg++, and Fe++ showed an activating effect.
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  • Part I. (±)-Mellein
    Masanao MATSUI, Kenji MORI, Seitetsu ARASAKI
    1964 Volume 28 Issue 12 Pages 896-899
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • Part III. Synthesis of Methyl 2-O-Acetyl-3-O-mesyl-5-O-benzyl-D-xylofuranoside and Solvolysis of its Sulfonyl Ester
    Hiroyoshi KUZUHARA, Sakae EMOTO
    1964 Volume 28 Issue 12 Pages 900-907
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • Gaschromatogramm der bei der Blätteralkohol-reaktion erhaltenen Alkohole
    Von Minoru OHNO, Akikazu HATANAKA
    1964 Volume 28 Issue 12 Pages 908-909
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • Herstellung des 2-Butyl-octylalkohols bei Blätteralkohol-reaktion
    Von Akikazu HATANAKA, Minoru OHNO
    1964 Volume 28 Issue 12 Pages 910-913
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • Takeaki KATO, Kenzo UEDA, Keimei FUJIMOTO
    1964 Volume 28 Issue 12 Pages 914-915
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • 1964 Volume 28 Issue 12 Pages e3a
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • 1964 Volume 28 Issue 12 Pages e3b
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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  • 1964 Volume 28 Issue 12 Pages e3c
    Published: 1964
    Released on J-STAGE: November 27, 2008
    JOURNAL FREE ACCESS
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