The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Search
Advanced search
OR
Browse
Search
Volume 45, Issue 5
Displaying 1-10 of 10 articles from this issue
Show all abstracts
    • |<
    • <
    • 1
    • >
    • >|
  • TERMINAL OXIDATION SYSTEM IN YEAST
    I. ON THE ROLE OF ACTION OF CYTOCHROME b2
    TATEO YAMANAKA, TAKEKAZU HORIO, KAZUO OKUNUKI
    1958 Volume 45 Issue 5 Pages 291-298
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    An enzyme preparation which contains cytochrome b2 has been prepared from baker's yeast. In the presence of the enzyme, ferricytochrome c can be reduced by lactate, malate, and TPNH. The cytochrome b2 involved in the enzyme preparation is also reduced by lactate, malate, and TPNH.
    These facts suggest that cytochrome b2 has a pivotal action in an electron-transferring system in baker's yeast.
    We would like to express our hearty thanks to Oriental Yeast, Co., Ltd. for their supply of pressed baker's yeast, and to Mr. K. Fujii* for his guidance. We should like to thank our colleagues Messrs. T. Higashi, M. Nozaki, J. Yamashit a and H. Mizushima for helpful discussions during the course of this work.
    View full abstract
    Download PDF (421K)
  • MICROBIOLOGICAL DEGRADATION OF BILE ACIDS
    XVII. SUPPLEMENTARY STUDIES ON CHOLIC ACID DEGRADATION BY CORYNEBACTERIUM SP
    KEIZO TAMAKI
    1958 Volume 45 Issue 5 Pages 299-303
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    1. Microbiological transformation of cholic acid to 7α, 12α-dihydroxy-3-oxo-Δ4-cholenic acid by Corynebacterium sp. may take place either in a synthetic medium containing cholic acid as the sole source of carbon or in a medium containing glucose in addition to cholic acid as the carbon sources.
    2. 7α, 12α-Dihydroxy-3-oxo-Δ4-cholenic acid (III) 12α-hydroxy-3-oxo-Δ4, 6-choladienic acid (IV) were obtained as the degradation products of cholic acid by Corynebacterium sp., but the ultraviolet absorption data of the culture suggest that a conversion of the acid III to IV may be not an enzymatic reaction.
    The auther wishes to express his sincere thanks to Prof. T. Shimizu, Prof. S. Mizushima and Dr. S. Hayakava for their kind guidance throughout this research, and to Mr. Y. Matsui of Research Laboratory, Shionogi & Co., Ltd. for his help in measuring the infrared absorption spectra.
    View full abstract
    Download PDF (268K)
  • CRYSTALLINE BACTERIAL PROTEINASE
    III. COMPARISON OF CRYSTALLINE PROTEINASE OF BACILLUS SUBTILIS WITH CRYSTALLINE TRYPSIN
    BUNJI HAGIHARA, MASASHI NAKAI, HIROSHI MATSUBARA, TOSHIAKI KOMAKI, TAK ...
    1958 Volume 45 Issue 5 Pages 305-311
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    Stability at neutral pH, proteolytic activity measured by various assay methods, and course of digestion of casein and gelatin were compared between crystalline proteinase of Bac. subtilis, BPN', and crystalline trypsin. The time required to decrease 0.1 per cent solution of BPN' was about 30 times longer than that of trypsin. Activity of BPN' measured by casein or hemoglobin digestion methods, gelatin liquefying method and formol titration method using casein and gelatin as substrate, was 1.9-3.3 times stronger than that of trypsin, and milk clotting activity of BPN' was about 10 times stronger than trypsin.
    View full abstract
    Download PDF (402K)
  • A NEW COLORIMETRIC DETERMINATION METHOD OF SPHINGOSINE BASE IN LIPIDS
    TOSHIO SAKAGAMI
    1958 Volume 45 Issue 5 Pages 313-317
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    A colorimetric method of sphingosine base determination was devised. The principle was based on the colorimetric determination of higher fatty aldehyde produced by the oxidation of sphingosine base with lead tetraacetate.
    At first the experiment on free sphingosine base was carried out and it was shown that higher fatty aldehyde was quantitatively produced, in proportion to sphingosine base content, by the oxidation with lead tetraacetate. Furthermore, this method was found to be applicable to the determination of sphingosine base in lipids.
    Finally sphingosine base contents in human serum, brain, rat brain and liver were determined.
    The author wishes to express his deep indebtedness to Prof. K. Ohno for his helpful criticism on this work.
    View full abstract
    Download PDF (258K)
  • PHOTOPHOSPHORYLATION BY CHLOROPLASTS
    TAKAO OHMURA
    1958 Volume 45 Issue 5 Pages 319-331
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    Both the chloroplast fragments and whole chloroplasts fractions had the activities of photosynthetic phosphorylation. The activities of the two fractions were almost equal when calculated on unit amount of chlorophyll. Neither removal of oxygen nor addition of menadione did not produce any accelerating effect on the reaction. From the effect of DNP, it was concluded that the photophosphorylation was a distinct phosphorylation reaction different from oxidative phosphorylation of mitochondria.
    The author wishes to express his gratitude to Prof. S. Funahashi of the Faculty of Agriculture, University of Tokyo, for his interest in this work.
    View full abstract
    Download PDF (814K)
  • AN APPARATUS FOR STUDY OF THIXOTROP_??_OF BIOCOLLOID
    HIROYUKI MATSUMIYA, MASAHIKO TANISAKA
    1958 Volume 45 Issue 5 Pages 333-340
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    An apparatus for measurements of the dependency of viscosity, intensity of flow birefringence and relaxation of birefringence on the velocity gradient was constructed, employing a sample cell of a capillary type. With this apparatus, relaxation longer than 0.2 msec could be recorded.
    Our thanks are due to Dr. Tonomura of Research Institute for Catalysis for his instruction and valuable advices during the course of this work and the preparation of the manuscript and also to Mr. Kabashima for his skillfull technical assistance.
    View full abstract
    Download PDF (432K)
  • THE STRUCTURE OF CYTOCHROME C
    II. PROPERTIES OF ACETYLATED CYTOCHROME C
    SHIGEKI MINAKAMI, KOITI TITANI, HISAYUKI ISHIKURA
    1958 Volume 45 Issue 5 Pages 341-348
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    1. Cytochrome c was acetylated with acetic anhydride and electro-phoretically homogeneous derivatives acetylated to several degrees were obtained.
    2. Acetylated cytochrome c had several physicochemical properties different from the native one due to the loss of positive electric charges : electrophoretic mobility, non-absorption on resin IRC-50 or cellophane dialysis membrane and the diminution of solubility in acidic medium.
    3. The absorption spectra were not modified by the acetylation. Acetylated cytochrome c was readily autoxidizable in air but did not combine with carbon monoxide.
    4. Acetylated cytochrome c did not accelerate oxygen uptake in succinic oxidase system if measured manometrically. However, it could be oxidized and reduced enzymatically, though the efficiency was reduced by the treatment.
    5. Ascorbic acid oxidase and hydroxylamine reductase activities were negligible in the acetylated derivative.
    The authors wish to express their thanks to Prof. S. Akabori and Prof. H. Yoshikawa for constant guidances in the course of the work. Thanks are alse due to Prof. Y. Yoneyama and Dr. M. Ishimoto for their valuable discussions.
    View full abstract
    Download PDF (505K)
  • TURBIDOMETRIC TITRATION OF SERUM-PROTEIN
    II. SPECIES SPFCIFICITY OF SERUM ALBUMIN
    MASARU SOGAMI
    1958 Volume 45 Issue 5 Pages 349-358
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    The author investigated the species specificity of serum albumin and serum of man, rabbit goat and beef, using turbidometric titration and paperelectrophoresis. The results were as follows.
    1. The turbidometric titration of serum albumin had many peaks and allow to detect very subtle differences (as species specific) among different .species (Fig. 4).
    2. In order to obtain accurate turbidometric diagram, special care must be payed for the experimental conditions of serum separation, especially on the temperature influence upon the turbidometric diagram of serum albumin as illustrated in Scheme 1 and Fig. 5.
    3. Paper electrophoretic patterns of serum showed differences among man, rabbit and goat.
    The author wishes to thank Prof. K. Sasagawa and Assist. Prof. Y. Tamura, (Department of Physiology, Faculty of Medicine, Kyoto University) for their advice to my investigation. And also, the author wishes to thank Prof. T. Yamamoto Dr. M. Yamamoto (Department of Quantum Chemistry, Faculty of Science, Kyoto University), Prof. G. Wakizaka, Dr. K. Torizuka (Department of Internal Medicine, Faculty of Medicine, Kyoto University), Dr. H. Kiho, Dr. K. Kawai (Department of Physics, Faculty of Science, Kyoto University) and Dr. Y. Momotani (Department of Botany, Faculty of Science, Kyoto University) for their excellent discussion.
    View full abstract
    Download PDF (463K)
  • ACRIDINE SALT OF FLAVINMONONUCLEOTIDE
    KIYOSHI FUJISAWA
    1958 Volume 45 Issue 5 Pages 359-361
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Download PDF (733K)
  • MALONATE METABOLISM IN HUMAN PLACENTA
    NORIMASA HOSOYA, NOBUKO KAWADA
    1958 Volume 45 Issue 5 Pages 363-365
    Published: May 25, 1958
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Download PDF (146K)
    • |<
    • <
    • 1
    • >
    • >|
feedback
 Top