The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Volume 57, Issue 1
Displaying 1-16 of 16 articles from this issue
  • JUNICHI TAKEDA
    1965 Volume 57 Issue 1 Pages 1-6
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Aus dem Muskel von Natrix tigrina tigrina wurden Ophidin and Carnosin kristal-linisch dargestellt, and sie wurden durch Analy-se and Papierchromatographie identifiziert.
    2. Lysin, Histidin, Kreatin, Kreatinin and Taurin wurden in freier Form oder in Salzen kristallinisch dargestellt.
    3. Auf dem Papierchromatogramm zeigte sich, dass Glutaminsäure, Glycin, Prolin, Ala-nin, Cystin, Leucin (Isoleucin), Valin, Phenyl-alanin, Methionin, Tyrosin in freier Form vorkommen. Die Anwesenheit des ungebun-denen β-Alanin and der γ-Aminobuttersaure wurde auch in den Muskeln von Natrix tigrina tigrina erwiesen.
    4. Aus der von Lysin abfiltrierten Frak-tion konnte ein kristallinisches Pikrolonat iso-liert werden. Für diesen Körper werden die summarische Formeln C5H14ON2•(C10H8O5N4) H2O and C5H14ON2•(C6H3O7N3)2 aus Analy-senwerten des Pikrolonates and Pikrates ange-nommen, woraus man nur vermuten konnte, dass Hydroxycadaverin fur diesen Korper zur Diskussion gestellt wird.
    Herrn Prof. Dr. Sh. Tsunoo spreche ich hiermit für seine freundliche Anleitung bei der Ausfuhrung dieser Arbeit meinen verbindtichsten Dank aus. Herren Musashi and Horisaka danke ich für sorgfältige Mitarbeit.
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  • NARIMASA SAITO
    1965 Volume 57 Issue 1 Pages 7-13
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Br. fuscum was cultured for 22 hours at 30°C with shaking in a 5% glucose medium, and the cytoplasmic volume of the cell was measured by electron microscope.
    2. Glycolytic intermediates and nucleo-tides were extracted with TCA from the cell and their levels in the cytoplasmic fraction were evaluated after ion exchange chromato-graphic procedures.
    3. The experimental results showed that, generally, the amounts of free sugars such as glucose, DHA, ketohexose, etc. rose above those of the other phosphate esters.
    4. FDP was found to be accumulated at the highest level of all the glycolytic sugar phosphates, and followed by 2-PGA and G 6 P.
    5. It was also observed that cytoplasmic solution abounded in phosphorus compounds such as ADP, Pi, ATP, UDP and its com-plexes, NAD, GTP, etc.
    The author wishes to express his sincerest thanks to Prof. K. Arima and Prof. Y. Ikeda of the Univer-sity of Tokyo for their kind guidances throughout this work. Great indebtedness is also acknowledged to Dr. S. Mizushima for his valuable suggestions.
    The author also wishes to thank Dr. M. Mogi and Dr. N. Iguchi for their kind advices and en-couragements.
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  • TOMOJI SUZUKI, YUKIO MIZUSHIMA, TADASHI SATO, SADAAKI IWANAGA
    1965 Volume 57 Issue 1 Pages 14-21
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    The protein precursor of bradykinin and kallidin has been purified from bovine blood. The purification procedure, which has good reproducibility, consisted of fractionation with ammonium sulfate, heat treatment, chro-matography on DEAE-cellulose, pH treatment and chromatography on CM-cellulose. The average yield of bradykininogen was about 100 mg. dry weight from 8 liters of bovine blood. Ultracentrifugation and moving bound-ary electrophoresis of the purified bradykini-nogen showed a nearly homogeneous single peak. Trypsin, venom enzyme and hog pan-creatic kallikrein acted on the purified brady-kininogen and released contractile materials for the guinea pig ileum. These active mate-rials formed enzymatically have been identified as bradykinin in the case of trypsin or venom enzyme, and as kallidin in the case of kalli-krein.
    We are greatly indebted to Dr. D. F. Elliott of National Institute for Medical Research, Mill Hill, London, for the valuable sample of synthetic brady-kinin. We are further obliged to Dr. S. Matushima of Teikoku Hormone Manufacturing Co., Tokyo, for kallikrein and to Dr. Y. Kawade for the ultracentri-fugal examinations.
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  • I. Monomer and Dimer Interconversion
    KAZUO MOTONAGA, EIICHI MISAKA, EIICHI NAKAJIMA, SHOGO UEDA, KAZUO NAKA ...
    1965 Volume 57 Issue 1 Pages 22-28
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Among Saccharomyces oviformis M2 cytochrome c, sulfhydryl type (cyc. c-SH), thiosulfate type (cyt. c-S-SO3-), and disulfide type (cyt.c-S-S-cyt. c) could be converted into each other, and the reaction of the sulfhydryl group in cytochrome c can be explained as follows:
    cyt. c-S-+Cu++→cyt.c-S-S-cyt.c
    cyt. c-S-S-cyt.c+RS--2cyt.c-S-+RSSR
    cyt.c-S-S-cyt.c+SO3--→cyt.c-S-+cyt.c-S-SO3-
    cyt.c-S-SO3-+RS-→cyt.c-S-+RSSR+SO3--
    And there were no fundamental differences in the enzymatic activity and the absorption specta among them.
    The authors wish to thank Dr. K. Kakiuchi, Institute for Protein Research, Osaka University, for the molecular weight measurements, and Dr. G. Meshizuka and his collaborators, Tokyo Metropolitan Isotope Centre, for their technical advice and assistance.
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  • II. Proteinase Digestion and Ultraviolet Difference Spectra
    KAZUO MOTONAGA, HAMAKO KATANO, KAZUO NAKANISHI
    1965 Volume 57 Issue 1 Pages 29-33
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Saccharomyces oviformis M2 cytochrome c, sulfhydryl type or non-sulfhydryl type were digested by proteinases, and non-sulfhydryl type cytochrome c was digested much faster than sulfhydryl types.
    2. The difference spectra of urea treated and untreated cytochrome c were examined for sulfhydryl type group or non-sulfhydryl type group. The absolute value of ΔA at minima in the difference spectra obtained from sulfhydryl type cytochrome c were smaller than the non-sulfhydryl type cyto-chrome c. These results coincide with the results of the proteinase digestion.
    3. The changes of the proteinase digestability and of ultraviolet difference spectra with urea treatment were reversible. And the three types of cytochrome c of Saccharo-myces oviformis M2 (sulfhydryl, disulfide, and thiosulfate type) were freely interconverted into each other. The conformation of cyto-chrome c in its sulfhydryl type was rather rigid, but the conformation was converted to a loose form when any reagents (including sulfhydryl type cytochrome c itself) were combined to this sulfhydryl group.
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  • I. Gluc-Amylase-Phenyl-α-maltoside or Maltose System
    SÔZABURO ONO, KEITARO HIROMI, ZEN-ICHIRO HAMAUZU
    1965 Volume 57 Issue 1 Pages 34-38
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Reactions of phenyl α-maltoside or an equilibrium mixture of maltose catalyzed by glut-amylase of Rh. Delemar has been followed simultaneously by the optical rotation mea-surement and reducing power measurement at pH 4.5 (0.02 M acetate buffer) and 25°C.
    A general method for following the time course of the amylase reaction of simple sub-strate and determining quantitatively the anomeric form of the hydrolytic product has been proposed.
    Calculations show that glucose formed from non-reducing glucose residue is exclu-sively of β-form. These results indicate that the Walden inversion takes place inevitably at the time of reaction.
    The authors wish to express their thanks to Prof. J. Fukumoto and Dr. Y. Tsujisaka of the Osaka Municipal Technical Research Institute who supplied them crystalline gluc-amylase of Rh. Delemar.
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  • II. Gluc-Amylase-Isomaltose System
    ZEN-ICHIRO HAMAUZU, KEITARO HIROMI, SÔZABURO ONO
    1965 Volume 57 Issue 1 Pages 39-41
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Gluc-amylase (of Rh. Delemar)-catalyzed reaction for isomaltose having α-1, 6 glucosidic linkage has been carried out under the condi-tions of pH 4.5 (0.02 M acetate buffer) and 25°C throughout.
    It has been demonstrated that only β-glucose is formed from non-reducing glucose residue when α-1, 6 glucosidic linkage was hydrolyzed by the enzyme.
    The authors wish to express their thanks to Prof. K. Shibasaki of Tohoku University who supplied them isomaltose and to Mr.K. Takahashi who prepared glueamylase.
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  • III. Taka-Amylase A-Phenyl-α-maltoside System
    ZEN-ICHIRO HAMAUZU, KEITARO HIROMI, SÔZABURO ONO
    1965 Volume 57 Issue 1 Pages 42-44
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Hydrolytic reaction of phenyl α-maltoside catalyzed by crystalline Taka-amylase A was carried out at pH 5.1 (0.05M acetate buffer) and at 35°C. By means of simultaneous measurement of reducing power, amount of phenol and optical rotation, the time courses of α-and β-maltose, phenol and phenyl α-maltoside of the reaction system have been obtained.
    It has been demonstrated that α-maltose is released exclusively from this substrate.
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  • XIII. Interpretation of the Anomalous Spectral Behaviors of Cytochrome a
    YUTAKA ORII, KAZUO OKUNUKI
    1965 Volume 57 Issue 1 Pages 45-54
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. By titration of reduced cytochrome a with oxygen the absorption curve of a true oxygenated form of cytochrome a could be obtained.
    2. The effects of native and guanidinated cytochrome c's and ferricyanide on oxygenated cytochrome a were compared with that of acetylated and succinylated cytochrome c's and it was confirmed that one of the dual functions of cytochrome c in the oxidase re-action is that it catalyzes the conversion of the oxygenated to the oxidized form.
    3. The differences in the absorbancy changes of cytochrome a at 605 mμ and 444 mμ on addition of ascorbate to the preparation were interpreted in terms of a single compo-nent in the cytochrome oxidase, cytochrome a, based on its cyclic change in its functional state. Kinetic results showed that ascorbate was effective only in reducing cytochrome a in contrast to the effect of cytochrome c, which transfers electron to cytochrome a nda also catalyzes the oxidation of the oxygenated form of cytochrome a.
    4. Interpretations of the spectral behaviors of an oxidase system composed of cytochromes a and c in the aerobic steady state were con-sistent with our view on the mechanism of the oxidase reaction.
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  • KOICHI YAGI, IKUKO SAKAKIBARA
    1965 Volume 57 Issue 1 Pages 55-63
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Actin polymerization was studied by the measurement of inorganic orthophosphate liberation from G-actin after the addition of MgCl2, CaCl2 and KCl. The time-course of phosphate liberation followed first order kine-tics, with respect to the G-actin concentration, but the dependence of the initial velocity on G-actin concentration was of the third order.
    2. Changes in light scattering and viscosity accompanied with actin polymerization were studied in various environments and at dif-ferent pH values. In contrast to the reaction of phosphate liberation, these changes did not follow any simple kinetics.
    3. The accelerating effects of myosin A and H-meromyosin on phosphate liberation from G-actin was studied in the presence of salts. The time course of phosphate liberation in the presence of these proteins also followed first order kinetics. The accelerating effect of H-meromyosin reached a maximum when the molar ratio of H-meromyosin to G-actin was 1:10.
    We wish to thank Dr. Y. Tonomura for many valuable suggestions and criticisms and Mr. H. Naka-mura for skilled technical assistance.
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  • YOSHIHIRO SOKAWA, FUJIO EGAMI
    1965 Volume 57 Issue 1 Pages 64-74
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. A protoplast membrane fraction of Streptococcus pyogenes S 8 was prepared.
    2. A hemolysin of streptolysin S nature was released from the membrane fraction by ATP and Mg++ in the presence of oligonu-cleotide or Tween 40.
    3. Contrary to the net synthesis by resting cells, the release was not inhibited by chloramphenicol, puromycin and strepto-mycin.
    4. The system consisting of the mem-brane fraction, ATP and Mg++ could lyse the rabbit erythrocytes. The hemolysis was not inhibited by cholesterol.
    5. From these observations, it was con-cluded that the hemolytic component of streptolysin S was released from the mem-brane fraction by ATP and Mg++. The hemolysin of streptolysin S nature obtained in the presence of oligonucleotide or Tween 40 is a complex of a hemolytic component (polypeptide) and a stabilizing component (oligonucleotide or Tween 40).
    6. For the release of hemolytic compo-nent from the membrane fraction, GTP, UTP, CTP, ADP and creatine phosphate-creatine kinase system were as effective as ATP. GDP, UDP, CDP, AMP, GMP, UMP, CMP, mal-tose and glucose were ineffective.
    7. For the release, Mg++ could be re-placed by Mn++, but not by Ca++. The latter was rather inhibitory for the reaction.
    8. The release of the hemolytic compo-nent by ATP and Mg++ could not be observed in the presence of trypsin. No inhibitory effect on the release of the hemolytic com-ponent was observed with RNases and several enzyme poisons such as PCMB et al.
    9. The hemolytic component was still retained in the membrane fraction prepared from resting cells preincubated in the presence of maltose. Chloramphenicol, puromycin and streptomycin inhibited the synthesis of the hemolytic component by resting cells. Peni-cilline G and mitomycin C had no effect.
    The present authors wish to express their sincere thanks to Dr. J. Koyama for his useful discussions.
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  • LXIV. The Isolation and the Chemistry of a New Bile Alcohol, 3α, 7α, 12α, 24ξ, 26-Pentahydroxybishomocholane from Rana Catesbiana Bile
    TARO KAZUNO, TAKAKO MASUI, KYUICHIRO OKUDA
    1965 Volume 57 Issue 1 Pages 75-80
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Bile salts of Rana catesbiana, when treat-ed with the dioxane-trichloacetic acid reagent for the isolation of bile alcohols from its sul-fates, yielded a new bile alcohol which is assumed to be 3α, 7α, 12α, 24ξ, 26-penta-hydroxybishomocholane by the chemical re-actions and the nuclear magnetic resonance spectrum.
    2. It was verified by synthesis that the new bile alcohol has structure (I) of 3α, 7α, 12α, 24ξ, 26-pentahydroxybishomocholane.
    3. A number of unsaturated bile alcohols obtained by alkaline hydrolysis of the same bile were missed in its acidic hydrolyzate.
    4. The presence of 3α, 7α, 12α, 24ξ, 26-pentahydroxybishomocholane in the frog bile suggests a mechanism of bile salt forma-tion different from that assumed so far in mammals.
    The authors wish to thank Dr. K. Takeda, Director of Shionogi Research Laboratory, Osaka, for his generous help in determination of nuclear magnetic resonance spectra.
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  • YOSHIMI OKADA, TAKAYASU YAGURA, TOKUJI IKENAKA, YUICHI YAMAMURA
    1965 Volume 57 Issue 1 Pages 81-88
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Rabbit anti-TAA γ-globulin was digested with papain and reduced with mercapto-ethanol. In this report, the immunochemical properties of rabbit anti-TAA fragments obtained by these methods were studied, and following results were obtained.
    1) Anti-TAA activity of F-1 of papain digest was much less than that of F-II, although no remarkable difference was observed in their amino acid contents,
    2) Maltosidase activity of TAA was increased by papain digests of anti-TAA, and the increase of maltosidase activity by F-I was higher than that by F-II. These data indicate the immunochmical differences between F-I and F-II of anti-TAA, and some interpretations and speculation of the mechanisms which give such differences are proposed.
    3) The chain A fraction from reduced anti-TAA seemed to have some of immunological activities of anti-TAA. However, there exists a possibility that the activities of the chain A fraction might be derived in part from possible contaminations of unreduced and reconstituted anti-TAA.
    4) The chain B fraction from reduced anti-TAA had no immunological activity.
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  • TOSHIO TAKAGI, TOSHIZO ISEMURA
    1965 Volume 57 Issue 1 Pages 89-95
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Effect of calcium ion on the refolding of reduced Taka-amylase A has been investigated. Presence of calcium ion in the reoxidation mixture was found to be necessary for the correct refolding. Addition of calcium ion equivalent to the reduced enzyme in molar basis was sufficient for the maximum recovery of enzymatic activity. The amount coincides well with that of the calcium atom which is firmly and specifically bound in native Taka-amylase A. Seemingly the calcium ion is bound to the polypeptide of the reduced en-zyme, and exerts so strong directive effect that the correct refolding occurs preferentially. This phenomenon is interesting as an example in which renaturation of a conjugated protein is controlled by its non-protein cofactor.
    The authors are gratefull to Sankyo Co., Ltd. for supplying “Taka-diastase Sankyo”, and to Dr. K. Hamaguchi and Mr. K. Yutani for their helpful discussions.
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  • MASASHI NAKAI, ZENRO MINAMI, TOSHIO YAMAZAKI, AKIRA TSUGITA
    1965 Volume 57 Issue 1 Pages 96-99
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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  • TOMOTAKA SHINODA
    1965 Volume 57 Issue 1 Pages 100-102
    Published: January 25, 1965
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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