SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
Volume 7, Issue 1
Displaying 1-4 of 4 articles from this issue
  • Report III. Protein-bounding-Polysaccaride and Cholesterol of Serum and Ascites
    Hideo Thukada
    1960Volume 7Issue 1 Pages 1-10
    Published: October 15, 1960
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Examing the changes of Cholesterol and Proteincompounding polysaccharide in Serum and Ascites under carcinomatic state, and ones of anemia, Hypoproteinemia and liber disfunction, the following results were gainedl.
    1) The increase of Protein-Compounding polysaccharide in Serum and Ascites is parallel with γ-glycoprotein. There are many protein cocpoundmg polysaccharide and γ-globlin in the sediment of Ascites of Yoshida's Sarcom contained tumor cells, Therefore, the increase of Protein compounding polysaccharide in Serum and Ascites considers the destruction of tumor cells one of main causes.
    2) Cholesterol in Serum and ascites increases, brt B fraction (lipoprotein) shows lower level and the parallel relation in both is not recognized.
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  • S. Tuzioka
    1960Volume 7Issue 1 Pages 11-18
    Published: October 15, 1960
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Proof the formation of enzyme-substrate complex between DPN-specific dehydrogenases and coenzymes as well as their substrates were carried out by the method of “crossing paper electrophoresis”.
    The enzymes used were lactic dehydrogenase (LDH), malic dehydrogenase (MDH), alcohol dehydrogenase (ADH), and glycerinaldehyde-3-phosphate dehydrogenase (GDH). On a filter paper, an enzyme solution was applied on a line drawn in parallel to the direction of the electrical field and a solution of substrate or coenzyme was applied on a line parpendicular to the former. After the electrophoresis the line of the substrate or coenzyme became hollow at the point of crossing with the line of enzyme. Thus the direct interaction and therefore the formation of complex between the enzyme and substrate as well as coenzymes were demonstrated with all the enzymes tested.
    In regard to the substrates, lactic and pyruvic acids were applied to LDH, and malic acid to MDH, but to ADH and GDH no substrate was applied. On the other hand the preparation used of MDH was not pure, so that the proof in this case can not be regarded as complete.
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  • Naoya Yamamoto
    1960Volume 7Issue 1 Pages 19-25
    Published: October 15, 1960
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    The venom of the Japanese viper, Agkistrodon halys (Pallas), contained at least seven components, which could be distinguished electrophoretically.
    By the one-dimensional crossing paper electrophoresis, it could be demonstrated that the viper venom reacted with its homologous horse antiserum to form at least six lines of precipitate.
    By the two-dimensional method, crossing diagrams were obtained. One of the crossing diagrams of the viper venom showed no less than twenty-one peaks of the lines of precipitate, which should correspond to the same number of antigens and antibodies, respectively. From the diagram obtained, the distribution of the antigens in the fractions of the viper venom and that of the antibodies in the antiserum were elucidated.
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  • 1960Volume 7Issue 1 Pages 26-34
    Published: October 15, 1960
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
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