Nippon Nōgeikagaku Kaishi
Online ISSN : 1883-6844
Print ISSN : 0002-1407
ISSN-L : 0002-1407
Volume 51, Issue 9
Displaying 1-11 of 11 articles from this issue
  • Ryoichi SHIRAI, Koitsu HIROTA, Takeichi SAKAGUCHI
    1977 Volume 51 Issue 9 Pages 527-530
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Free cyanide contents in loquat endosperm and mesocarp were determined to be 203±13 ppm and 0.22±0.08 ppm respectively.
    The cyanide metabolizing activity was partially purified about 430-fold by ammonium sulfate precipitation, Sephadex G-100 gel filtration and isoelectric focusing. The optimum pH for this activity was 8.0. Stoichiometric NH3 liberation from CN- was observed using the partially purified fraction.
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  • Ryoichi SHIRAI
    1977 Volume 51 Issue 9 Pages 531-534
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    The partially purified active fraction which metabolized cyanide in mesocarp of loquat that had been prepared as described in the previous paper was found to contain at least three enzymes. When [14C]-NaCN was used as substrate, two metabolic products were detected by papar chromatography with three solvent systems. Main peak coresponded to authentic [14C]-formate and the other coresponded to authentic [14C]-formamide.
    When [14C]-formamide was used as substrate, [14C]-formate also appeared as major peak and another peak X was detected. Formate formation from formamide and peak X were diluted by non-radioactive formaldoxime, therefore X may be formaldoxime.
    From these observation, it seems most likely that the following metabolic flow occurs in the mesocarp of loquat.
    CN-+H2O→H-_??_-NH2→(H2C=NOH)H2O→HCOOH+NH3
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  • Takako YOKOZAWA, Kumiko KANAI, Hikokichi OURA
    1977 Volume 51 Issue 9 Pages 535-541
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    The influence of dietary composition on uric acid metabolism was studied in the rat, and experimental results are summarized as follows: (1) The circadian variation of serum uric acid was observed in rats fed on a 25% casein diet. When rats were fed freely on a 25% casein diet, the level of serum uric acid was highest at 2 p. m. and lowest at 2 a. m. On the other hand, the circadian rhythm of enzyme activity was observed both in rats fed on a 25% and 70% casein diet. That is, the activity of xanthine oxidase showed a circadian variation with the same pattern as that of uric acid. Uricase activity exhibited a circadian fluctuation, with the highest: activity at 10 a. m. and the lowest at 6 p. m. (2) With yeast diet, serum uric acid showed a trough at 6 p. m. and a peak at 6 a. m. and the phase of the rhythm shifted with respect to that of rats fed on a 25% casein diet. The circadian rhythm was also observed in guanine deaminase activity.
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  • Setsuko KOBAYASHI, Kazumi ARAKI, Kiyoshi NAKAYAMA
    1977 Volume 51 Issue 9 Pages 543-550
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    A urocanase-deficient mutant KY 10550 was derived from a wild-type strain of Brevibacterium ammoniagenes ATCC 6872. It quantitatively converted L-histidine into urocanic acid.
    A 2-thiazo-DL-alanine (histidine analog)-resistant derivative of KY 10550, designated as UTA-55, accumulated 200 μg/ml of urocanic acid in a culture medium containing 15% sugar without supplemention of L-histidine. The urocanic acid productivity of UTA-55 was improved by successive addition of resistant markers; higher histidine analogs-resistance, purine analogs-resistance and streptomycin-resistance. Finally selected mutant strain FTGSA-7 accumlated 7.3mg/ml of urocanic acid.
    In the cource of the strain improvement, the mutants which accumulate L-histidine, imidazolelactate, imidazoleacetate or other substances were obtained.
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  • Hideyuki KOBAYASHI, Mitsutoshi NAKAGAWA, Isei NAKAMURA
    1977 Volume 51 Issue 9 Pages 551-559
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    This paper deals with process development studies on wood saccharification using strong sulfuric acid and phosphate rock for producing itaconic acid, in which process studies on recovery of disodium phosphate from the wood hydrolyzate containing phosphoric acid and on itaconic acid fermentation of the refined wood hydrolyzate are involved.
    The synthetically prepared sugar mixture solutions simulating several kinds of wood carbohydrate composition and wood hydrolyzate containing phosphoric acid have successfully been proved to give excellent yields of the acid by shake culture.
    Ten ppm of 5 valent arsenic compound inhibited Aspergillus terreus K 26 used for this fermentation test but it can be removed by a simple anion exchange operation as pretreatment of the wood hydrolyzate.
    For minimizing anion exchange capacity of the wood hydrolyzate, extraction of AcOH by tributyl phosphate and precipitation of salts of inorganic impurities at several steps of pH by neutralizing with Na2CO3 were performed.
    Purification process involves orthodox procedure described by Waggaman(1) and electrodialysis process for concentrating wood sugar mixture and preliminary refining of phosphoric acid.
    Amount of residual arsenic compounds in disodium phosphate crystals, which is allowed by JIS standards, was found less than 0.8 ppm.
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  • Ryuhei FUNABIKI, Yoshiro ITO, Akira ISHII, Ryuichiro HARADA, Nobuhiro ...
    1977 Volume 51 Issue 9 Pages 561-567
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Adult rats were once fed the test diets containing the different amount of fat component in two hours after being adapted to the meal-feeding schedule. The animals were decapitated at post-prandial stage and the glycogen content, phosphorylase activities were measured in skeletal muscle. Blood glucose and serum free fatty acid levels were also measured. An increase in the amount of fat component of the diet caused to decrease the glycogen content in skeletal muscle, along with the increase in the levels of serum free fatty acids which are thought to inhibit the uptake of blood glucose to the muscle cells. The phosphorylase activity in skeletal muscle exhibited a biphasic change with the variation in the amount of dietary fat component. Up to the fifty calorie per cent of the dietary fat component, the phosphorylase activity exhibited an increase, but over the fifty per cent, the activity turned to decrease in accordance with the decrease in declined tendency of glycogen deposition in skeletal muscle.
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  • Yoshiharu ETO, Shigeko NISHIOKA, Hiroyuki HORITSU, Mikio TOMOYEDA
    1977 Volume 51 Issue 9 Pages 569-571
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Four kinds of bacteria, which metabolized dehydroacetic acid, were isolated from mid-air and soil using enrichment cultivation containing dehydroacetic acid in the medium as a sole source of carbon. Among those bacteria, two kinds of bacteria, C-5-1 from mid-air and M-1 from soil, were designated as Pseudomonas sp. C-5-1 and Pseudomonas sp. M-1, respectively. It was found that degradation of dehydroacetic acid by Pseudomonas sp. C-5-1 was more rapid than that of Pseudomonas sp. M-1.
    The metabolic pathway of dehydroacetic acid by both strains was assumed as follows: dehydroacetic acid→triacetic acid lactone→triacetic acid→acetic acid→TCA cycle. Furthermore, the accumulation of triacetic acid by Pseudomonas sp. M-1 was strongly affected by the presence of ammonium nitrate in culture medium, but with Pseudomonas sp. C-5-1 such an effect was not observed.
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  • Tsuneo UCHIDA, Kenji ISHII
    1977 Volume 51 Issue 9 Pages 573-574
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Binding of Acid Red (an artificial food color) with soybean proteins was observed by changing pH from 6.8 to 1.0. The absorption maximum of Acid Red (at 566 nm in aqueous solution) showed a “red shift” by binding with soybean water-extracted protein and with acid-precipitated protein. The “red shift” was increased with decreasing pH from 6.8 to 2.2. Owing to acid-induced conformation changes in the soybean proteins, binding of Acid Red with the proteins was accelerated by decreasing pH and it became the greatest at pH 2.2. Difference spectra of Acid Red caused by binding with the proteins varied greatly with a decrease in pH from 3.8 to 2.2. However, no marked changes in “red shift” difference spectra and binding of Acid Red with the soybean proteins were observed at pH 1.0_??_2.2.
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  • 1977 Volume 51 Issue 9 Pages N153
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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  • Kazue ASO
    1977 Volume 51 Issue 9 Pages R83-R89
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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  • Yasushi SATO
    1977 Volume 51 Issue 9 Pages R91-R100
    Published: 1977
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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