The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Volume 44, Issue 8
Displaying 1-9 of 9 articles from this issue
  • SETURO FUJII, KIKUO ARAKAWA, NOBUHIKO AOYAGI
    1957 Volume 44 Issue 8 Pages 471-476
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Dipeptides were oxidized by the action of HIO4 in a neutral medium.
    2. Dipeptide containing hydroxyamino acid residue at its N-terminal was oxidized at 15° as readily as serine itself and gave NH3, RCHO, and glyoxyl-amino acid as the oxidation products.
    3. Dipeptide containing hydroxyamino acid residue at its C-terminal was not easily oxidized, and produced slowly amino acid amide, RCHO and glyoxylic acid when heated.
    4. Under such condition of heating, however, oxidation and splitting took place also in dipeptides not containing hydroxyamino acid residue, though they were much slowly oxidized than one containing it.
    The authors are indebted to Dr. R. Hirohata, professor of the department, for his valuable advices and encouragement during this work.
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  • III. A COMPARATIVE STUDY AMONG DIFFERENT KINDS OF MAMMALS
    MAKOTO NAKAO, ISAMU YANAGISAWA, HARUHISA YOSHIKAWA
    1957 Volume 44 Issue 8 Pages 477-480
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    A distinct qualtative difference in the metabolic pattern of PAS was demonstrated among human being, dog, rabbit, rat and mouse.
    Man excreted all the nine metabolic products. Dog excreted PAS, COOH-glucuronide, sulfate conjugate and the unknown glucuronide; rabbit PAS, N-acetyl-PAS, COOH-glucuronide, OH-glucuronide and the unknown glucuronide; rat and mouse PAS, N-acetyl-PAS, COOH-glucuronide and the unknown glucuronide.
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  • RYOITI SHUKUYA, KONOE WATANABE
    1957 Volume 44 Issue 8 Pages 481-489
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. It has been shown that the hydrolysis of benzoyl-L-arginine amide by trypsin does not follow the conventional first order kinetics. The constant value of k3 which is independent of both enzyme and sub-strate concentration was obtained from integration of Michaelis-Menten equation.
    2. The existence of a group with pK'H=6.28 at 30° and the heat of ionization=7.1 Kcal. mole-1 in trypsin molecule was assumed from the pH dependence on the catalytic activity of trypsin. These values were very close to the figures quoted by Gutfreund.
    3. The temperature dependence of the trypsin catalyzed reaction was observed and the heats of enzyme-substrate complex formation and thet of the activation were calculated as 5.9 and 12.3 Kcal. mole-1, respectively.
    The authors indebted to Prof. K. Kaziro for his continuous help and stimulating discussion. The authors also express their gratitude to the Ministry of Education for the aid of the Scientific Research Fund.
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  • XV. EFFECT OF XANTHURENIC ACID ON HEXOKINASE ACTIVITY
    YAHITO KOTAKE, YUKIO SHIBATA, ICHIRO NAGAYAMA, GENZABURO ABE
    1957 Volume 44 Issue 8 Pages 491-498
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    From the experiments stated above, xanthurenic acid can unmis-takably inhibit hexokinase activity and it is highly possible to imagine that what has much to do with the inhibition may be either Mg_??_or -SH system. In either case, however, it is safe to consider that since glycosuria due to xanthurenic acid can be found to be identical with glycosuria caused by the action of alloxan, xanthurenic acid has been confirmed to be a diabetogenic substance.
    1. Xanthurenic acid inhibits phosphorylation of hexose in rat liver.
    2. It inhibits also animal and yeast hexokinase activity.
    3. 4-OH-8-OCH3-quinolin-2-carboxylic acid, kynurenic acid, an-thranilic acid, 5-OH-anthranilic acid and cystein protect hexokinase activity against the inhibitive action of xanthurenic acid.
    The authors wish to express their sincere thanks to Prof. Y. Kotake for his con-stamt encouragement and to Prof. K. Kodama for his kind revision and to Prof. K. Okunuki, Mr. K. Iwas a and Mr. F. Imamoto of the Department of Science of the Osaka University for their kind assistance in the preparation of hexokinase.
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  • I. THE C-TERMINAL RESIDUE OF CYTOCHROME C
    KOITI TITANI, HISAYUKI ISHIKURA, SHIGEKI MINAKAMI
    1957 Volume 44 Issue 8 Pages 499-503
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    The C-terminal amino acid of horse heart muscle, yeast and whale heart muscle cytochrome c was tested by hydrazinolysis method, and 1 mole of glutamic acid was detected per 1 mole of every cytochrome c.
    The authors wish to express their thanks to Prof. S. Akabori, Prof. H. Yoshi-kawa, Prof. K. Satake and Prof. Y. Yoney ama for constant guidances in the course of the work. Thanks are also due to Dr. K. Narita and Mr. K. Kusama for their kind technical advices.
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  • IV. THE CONVERSION OF PYRUVIC ACID TO ALANINE IN THE SILKWORM LARVA
    TOSHIFUMI FUKUDA
    1957 Volume 44 Issue 8 Pages 505-510
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    The present work was carried out, using sodium pyruvate-2-C14, to examine whether pyruvic acid is utilized for the synthesis of alanine in the silk by Bombyx mori.
    2. The isotope (C14) of the sodium pyruvate-2-C14 given to the silkworms appeared in the 2C position of the alanine isolated from the cocoon fibres produced by these silkworms.
    3. Alanine was synthesized from pyruvic acid in the presence of amino acids, especially glutamic acid or aspartic acid in all the silkglands, the alimentary cannal, the muscles and the fat tissues of the silkworm larvae.
    4. These facts seem to suggest that the conversion of pyruvic acid to alanine in the silkworm larva is of special importance in the synthesis of the alanine of the silk.
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  • I. STUDIES ON THE ACETONE INSOLUBLE FRACTION BY PAPER ELECTROPHORESIS
    KUNIHIKO SAITO, SHÛZO AKASHI
    1957 Volume 44 Issue 8 Pages 511-524
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The electrophoretic separation of phosphoglycerides in an organic buffer system was described, which was able to separate a trace amount of a synthetic mixture of phosphatidic acids, cephalin fraction and lecithin into its component lipids.
    2. The acetone insoluble fraction of the lipids from B. alcaligenes faecalis was analyzed in the same manner and it was fractionated into two parts, of which one was phosphatidic acids and the other phosphogly-cerides containing ethanolamine and polypeptides in a bound form.
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  • KEIZOO TSUSHIMA, GORO KIKUCHI, MICHIKO MAKITA, FUJIKO UCHIMURA, KOOZOO ...
    1957 Volume 44 Issue 8 Pages 525-533
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. When dicyanhematin reacted with H2O2 or with atmospheric oxygen in the presence of ascorbic acid, a product was obtained which is characterized by its absorption at 588 and 545-550mμ in its ferrous state. When the oxidation proceeded further, it gave rise of a second product which shows an absorption maximum at 618mμ in its ferrous state.
    2. Both products in their free state can combine with pyridine or globin. It is notable that their pyridine compounds possess their ab-sorption maxima rather at shorter wavelength side compared with those of their CN-compounds. But, in respect to the absorption figure as a whole, both compounds, pyridine and cyanide compound are in close resemblance.
    3. Both products are assumed to have the original closed ring structure. The second product bears a close resemblance to pseudo-hematin in their property though not in perfect identity. Both are stable in alkaline solution; they are not easily oxidizable by atmospheric oxygen.
    The present work was aided in part by the Scientific Research Fund of the Ministry of Education for which the authors wish to express their hearty gratitude.
    The present work was published partly in Japanese in the Journal of Japanese Biochemical Society (10).
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  • SHIGEKI MINAKAWI, KOITI TITANI, HISAYUKI ISHIKURA
    1957 Volume 44 Issue 8 Pages 535-536
    Published: August 25, 1957
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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