Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
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Volume 29, Issue 6
Displaying 1-17 of 17 articles from this issue
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  • Studies on the Metabolism of Aspergilli
    Part VI. Time Course of Changes of Several Enzymes during Endogenous Respiration
    Takeji MIZUNUMA
    1965 Volume 29 Issue 6 Pages 491-502
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.491
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    Studies were made on the time course of changes of several enzymes during endogenous respiration in the mycelia of Aspergillus sojae K. S.
    1) It was observed that the following enzymes found in the mycelia increased in activity more or less during endogenous respiration: glutamic dehydrogenase, glutamate-alanine transaminase, glutamate-aspartate transaminase, L-glutaminase, L-threonine de-aminase, L-amino acid oxidase, AMP de-aminase and adenosine deaminase.
    2) It was assumed that enzyme formation occurred as the result of glucose starvation or depression of carbohydrate metabolism during endogenous respiration of the mold mycelia on buffer solution.
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  • On the Mode of Action of Scopulariopsis brevicaulis Proteinase
    (Prot. II) on the Oxidized Insulin
    Tadaaki KISHIDA, Sadahiko YOSHIMURA
    1965 Volume 29 Issue 6 Pages 503-507
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.503
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    An attempt was made to examine the detailed specificity of crystalline Scopulariopsis brevicaulis (Prot. II) proteinase by using the oxidized A- and B-chain of bovine insulin, and the resulting peptides or amino acids in each hydrolyzate were qualitatively deter-mined by column chromatography.
    The present proteinase has rather a broader specificity in its action than trypsin or chymotrypsin, but a little more restrictive than that of Aspergillus oryzae or subtilopeptidase A.
    The cleavage in the A- and B-chains occurred rapidly at such bonds, where leucine, valine or glutamic acid is linked by its respective carboxyl group.
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  • On the Purification and some Properties of 5'-Adenylic Acid-Deaminating Enzyme from Microsporum audouini
    Kô AIDA, Shiau-ta CHUNG, Isamu SUZUKI, Tsutomu YAGI
    1965 Volume 29 Issue 6 Pages 508-514
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.508
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    From culture broth of Microsporum audouini, 5'-adenylic acid-deaminating enzyme has been purified to about 600-fold. The pH optimum was found to be 5.0 in acetate, 5.5 in succinate, 5.7 in citrate buffer. Velocity constant was 1.83×10-1 per minute. The optimal temperature was 40&C and activation energy was 15, 000 calories. Michaelis-Menten constant was 6×10-4M. This enzyme preparation removes amino groups of 5'-AMP, ADP and ATP quickly, of adenosine, 3'-AMP, 5'-deoxyAMP and NAD slowly, but adenine, 2, 6-diaminopurine, 2'-AMP and NADP were not deaminated. The enzyme activity was inhibited with F-, pCMB, Fe+++, Cu++ and Zn++
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  • Chemical Studies on Ninhydrin-Positive Compounds in Cured Tobacco Leaves
    Part II. Isolation of 1-Deoxy-l-L-Prolino-D-Fructose
    Hideo TOMITA, Masao NOGUCHI, Einosuke TAMAKI
    1965 Volume 29 Issue 6 Pages 515-519
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.515
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    1-Deoxy-l-L-prolino-D-fructose was isolated from flue-cured tobacco leaves in crystalline form. The structure was confirmed by comparison with synthetic compound.
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  • Studies on the Xylanase from Streptomyces
    Part I. Purification and some Properties of Xylanase from Streptomyces xylophagus nov. sp
    Hiroshi IIZUKA, Toshiro KAWAMINAMI
    1965 Volume 29 Issue 6 Pages 520-524
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.520
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    Xylanase from Streptomyces xylophagus nov. sp. has been purified by ammonium sulfate fractionation and chromatography on DEAE-cellulose column. The purification of the enzyme was 276-fold with a yield of 18.6% on the basis of the activity per weight of total nitrogen. The purified enzyme was homogeneous on moving-boundary electrophoresis. Optimum pH and temperature for the enzyme activity were 6.2 and 55_??_60°C, respectively. The enzyme was stable up to 40°C and in the range of pH from 5.3 to 7.3, but inactivated at higher than 50°C and at extreme pH values of 2.4 and 9.4. Hydrolyzed products of xylan by the enzyme were xylose and xylobiose.
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  • The After Effect of Irradiated Halogenophenol Solutions on the Viability of Escherichia coli
    Part I. Effect of Irradiation Conditions on the Radiation Induction of Bactericidal Activity
    Mitsuo NAMIKI, Akira MATSUYAMA
    1965 Volume 29 Issue 6 Pages 525-532
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.525
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    Gamma irradiation has been found to induce a remarkable bactericidal activity in an aqueous soltion of p-bromophenol even at the non-toxic lower concentrations, but not in a crystalline form or under a frozen state. Effects of concentration of reagents, temperature, pH, radiation dose, oxygen and some additives during irradiation on the radiation induction of bactericidal activity in the p-bromophenol solution were investigated. The results suggest that the induced activity is attributable to some long-life products, formed as a result of radiolysis of p-bromophenol and in coupling with radiolysis of water. The processes of formation and destruction of such bactericidal factor(s) were considerably influenced by several conditions during irradiation. Based on the experimental results, relationship between radiolysis process and induction of bactericidal activity was discussed.
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  • The After Effect of Irradiated Halogenophenol Solutions on the Viability of Escherichia coli
    Part II. Effect of After Irradiation Treatments on the Bactericidsal Activity of Irradiated p-Bromophenol Solution
    Mitsuo NAMIKI, Akira MATSUYAMA
    1965 Volume 29 Issue 6 Pages 533-539
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.533
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    Bactericidal activity of halogenophenol solution on E. coli was affected very much by post-irradiation treatments. The activity was significantly modified by heating at 80°C; it increased rapidly at an initial stage then decreased with increasing periods of heating until its complete disappearance. The addition of cysteine or sodium sulfite in the irradi-ated reagent solution prior to mixing with cells abolished the induced activity. The bactericidal factor is unstable at alkaline side, but is relatively stable at acidic side. The apparent induced activity depends on the cell concentration and the temperature at the period of contact with the irradiated reagent solution; no lethality was found at concen-trations above 108 cells per ml.
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  • Comparative Biochemical Studies on α-Glucosidases
    Part II. Substrate Specificity of an α-Glucosidase of Schizosaccharomyces pombe
    Seiya CHIBA, Tokuji SHIMOMURA
    1965 Volume 29 Issue 6 Pages 540-547
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.540
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    The properties of Schizosacch. pombe α-glucosidase have been studied.
    The preparation of α-glucosidase from Schizosacch. pombe was fractionated into three fractions of peak I, II and III by DEAE-cel-lulose column chromatography, but in this experiments Peak III was used as enzyme.
    The range of pH-optimum was 4.0_??_4.4 and optimal temperature was 45°C, The enzyme lost almost all the enzymatic activity at 55°C for 15min. and the range of pH-stability was 3.2_??_6.8 at 30°C for 20 hours.
    The enzyme was capable of hydrolyzing more readily malto-oligosaccharides in comparison with other various saccharides, and even malto-heptaose and -octaose were attacked feebly. The rate of hydrolysis decreased in the followihg order: maltose, isomaltose, phenyl-α-glucoside, panose and turanose.
    Accordingly, it was suggested that the sub-strate specificity of this enzyme was quite different from that of brewer's yeast (Sacch. cerevisiae) α-glucosidase, 7) and it was similar to that of crystalline mold α-glucosidase.8)
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  • A New Antifungal Antibiotic, Polcillin
    Sadafumi OMURA, Kazuo OKUMURA, Hiroshi NAKAYOSHI, Jiro SAWADA
    1965 Volume 29 Issue 6 Pages 548-557
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.548
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    1. A new polypeptide antibiotic given a name of polcillin was obtained from culture filtrates of newly isolated Bacillus subtilis TPR-2201.
    2. Identification of the strain, determina-tion of cultural condition, purification of the antibiotic, physicochemical properties and biological properties were described.
    3. Polcillin is an acidic compound which consists of aspartic acid, glutamic acid, serine, proline and tyrosine.
    4. It is easily soluble in water, lower alcohol, pyridine and wet acetone but insolu-ble in other organic solvents.
    5. The growth of fungi and yeasts are widely inhibited but most bacteria are not inhibited.
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  • Tea Leaf Polyphenol Oxidase
    Part I. Solubilization and Properties of the Structurally Bound Polyphenol Oxidase in Tea Leaves
    Tadakazu TAKEO
    1965 Volume 29 Issue 6 Pages 558-563
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.558
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    The large part of the polyphenol oxidase was solubilized from tea leaf homogenate by addition of Tween-80. After filtration of the solubilized polyphenol oxidase fraction through a Sephadex G-25 column and fractionation of the filtrate with ammonium sulfate, the specific activity of the solubilized enzyme increased about 4 to 5 times as much as that of tea leaf homogenate. Optimum pH of the solubilized enzyme was 5.5, and was almost the same as that of water-insoluble enzyme in the acetone powder. The minimum concentrations required for the maximum activity were about 5×10-3 M, 4.3×10-3 M, and 3×lO-3 M for d-catechin, l-epigallocatechin, and l-epigallocatechin-gallate, respectively. d-Catechin showed the highest activity among them. The enzyme activity was inhibited by potassium cyanide and sodium diethyldithiocarbamate.
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  • Polysaccharides of Soybean Seeds
    Part I. Polyasaccharide Constituents of “Hot-Water-Extract” Fraction of Soybean Seeds and an Arabinogalactan as its Major Component
    Makio MORIA
    1965 Volume 29 Issue 6 Pages 564-573
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.564
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    A polysaccharide fraction extracted from soybean seeds with boiling water was ex-amined by several fractionation methods on ultracentrifugal criteria. Four components were found by a column chromatography using TEAE-cellulose or by a paper electrophoresis. Acetone-precipitation, fractionation by conversion into acetyl derivative, and copper- com-plex-precipitation were unsatisfactory to fractionate into the components. The major com-ponent (70%) isolated was an arabinogalactan containing residues of arabinose and galactose in the approximate proportion of 1:2 and having molecular weight of 3.3×105.
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  • The Chromatography of “Myosin B” Prepared from Minced Rabbit Muscle on Triethylaminoethylcellulose
    Nobuhiko ARAKAWA, Akihiro OKITANI, Masao FUJIMAKI
    1965 Volume 29 Issue 6 Pages 574-580
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.574
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    The chromatography on Cellex D DEAE-SF (Bio-Rad Lab.) or TEAE-cellulose (Serva) equilibrated against 0.28 M KCl solution containing 0.02 M tris-HCl buffer at pH 8.0 was found to be suitable for the refinement of myosin B.
    The ultraviolet absorption spectrum and ATPase activity of the eluted fractions showed that “myosin B” was fractionated and purified by this technique, especially by the preferential removal of the fraction suggested as ribonucleic acid related substance.
    The chromatography may provide the effective way to investigate changes of “myosin B” during aging of meat.
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  • The Changes of “Myosin B” during Storage of Rabbit Muscle
    Part I. Physico-chemical Studies on “Myosin B.”
    Masao FUJIMAKI, Akihiro OKITANI, Nobuhiko ARAKAWA
    1965 Volume 29 Issue 6 Pages 581-588
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.581
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    The differences between myosin B extracted from fresh muscle with Weber-Edsall solution and myosin B type protein from the muscle stored at 4°C post-mortem were investigated by the measurement of ATPase activity, ATP-sensitivity, salting-out curves, chromatographic patterns on triethylaminoethyl (TEAE)-cellulose, viscosity and ultra-centrifugation diagrams. As compared with myosin B from fresh muscle and myosin B type protein from post-rigor muscle, myosin B type protein from rigor muscle showed relatively high values of ATPase activity, ATP-sensitivity and reduced viscosity, and moreover, was remarkably different in salting-out curves, precipitating gradually from ammonium sulfate of lower concentration than that in others. The differences between myosin B from fresh muscle and myosin B type protein from post-rigor muscle were clearly demonstrated by chromatography and sedimentation data.
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  • L-Glutamate Formation from Hydrocarbons by Microorganisms
    Takashi IGUCHI, Isao TAKEDA, Saburo SENO
    1965 Volume 29 Issue 6 Pages 589-590
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.589
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    Large quantities of L-glutamic acid from liquid paraffins by microorganisms were produced with an addition of penicillin to the growing culture, and the action of penicillin to the glutamate production was studied. One of main effects of penicillin seems to exist in the cellular permeability of L-glutamic acid.
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  • Biodegardation of Alkylbenzene Sulfonates (ABS) by Microorganisms in a Private Cesspool
    Kenkichi ÔBA, Shinichi TOMIYAMA
    1965 Volume 29 Issue 6 Pages 591-592
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.591
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  • The Evidence for the Formation of Chlorine Atoms in Neutral Aqueous Solution Containing Chloride Ions by Ionizing Radiations
    Akira MATSUYAMA, Mitsuo NAMIKI
    1965 Volume 29 Issue 6 Pages 593-594
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.593
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  • Synthesis of Dihydrohelminthosporic Acids and their Plant Growth-promoting Activity
    Saburo TAMURA, Akira SAKURAI
    1965 Volume 29 Issue 6 Pages 595-596
    Published: 1965
    Released on J-STAGE: November 27, 2008
    DOIhttps://doi.org/10.1271/bbb1961.29.595
    JOURNAL FREE ACCESS
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