The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
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Volume 60, Issue 6
Displaying 1-21 of 21 articles from this issue
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  • Studies on Lipoamide Dehydrogenase of Bakers' Yeast
    VIII. Inhibition of Enzyme Activity by Its Immune Antiserum
    EIICHI MISAKA
    1966 Volume 60 Issue 6 Pages 609-614
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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    Crystallized lipoamide dehydrogenase [EC 1.6.4.3] from Saccharomyces oviformis was found to be immunologically pure. The anti-enzyme antibody was readily formed by three or four subcutaneous injections of 3mg. of enzyme per week into rabbits. From the quantitative precipitin reaction, it was found that one mole of enzyme reacted with two moles of antibody at the equivalence zone of the antigen-antibody reaction. The NADH2-lipoamide and NADH2-menadione reductase activities decreased greatly when the enzyme combined with its antibody. However, the degree of inhibition did not change even when the enzyme reacted with more than two moles of antibody. The substrate NADH2 protected the enzyme slightly from inactivation by antibody. NAD had no protective effect.
    The author wishes to thank Dr. G. Sunagawa, the Director of these Laboratories, for encouragement during this investigation and Dr. K. Nakanishi for valuable advice and discussion.
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  • Studies on Elastoidin
    I. Some Chemical and Physical Properties of Elastoidin and Its Components
    SHIGERU KIMURA, MINORU KUBOTA
    1966 Volume 60 Issue 6 Pages 615-621
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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    1. Elastoidin, a member of the collagen complexes, proved to be a tightly bound substance of a characteristic collagen which may be extracted by pepsin treatment as a nativetype collagen molecule, and the non-collagenous protein which are probably attached to the terminal regions of collagen molecule.
    2. A small amount of the acid soluble protein, rich in tyrosine (19%) and cystine (0.42%) but poor in hydroxyproline (2.74%), was obtained from the elastoidin fiber by extraction with dilute acid, The acid soluble protein seems to be identical. with the noncollagenous protein reported by Gross and Dumsha in their amino acid compositions.
    3. Some cross linkages such as a disulfide linkage and a peroxide linkage formed by oxidation of two tyrosine residues, may possible explain the peculiar hydrothermal behaviour and insolubilization of elastoidin.
    The authors wish to thank Dr. M. Suyama, Ass. Prof. of Tokyo University of Fisheries for the amino acid analysis, Dr. K. Shibata, Prof. of Tokyo Institute of Technology for the ultracentrifugal analysis, and Dr. T. Hirano, Chief Research Member of Tokyo Metropolitan Isotope Center and Mr. S. Aida, Research Member of Japan Electron Optics Laboratory Co., Ltd. for the electron microscopical examinations.
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  • A Coupling Factor of Oxidative Phosphorylation without Adenosine Triphosphatase Activity from Beef Heart Mitochondria
    NOBUHITO SONE, BUNJI HAGIHARA
    1966 Volume 60 Issue 6 Pages 622-631
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    1. Preparation of a coupling factor and particles deficient of oxidative phosporylation were described. The coupling factor was solubilized by disrupting beef heart mitochondria with sonic oscillation in the presence of Mg2+ and Mn2+ and purified by fractionation with polyethylene glycol. The deficient particles were prepared by treating sonic fragments of mitochondria with 0.5M KCl.
    2. The purified factor stimulated the ATP-dependent NAD reduction and phosphorylation coupled to succinate and NADH oxidation in the KCl-particles. The factor also stimulated the ATP-dependent trans-hydrogenase reaction from NADH to NADP but did not stimulate this reaction driven by the energy generated by succinate oxidation.
    3. In the functions mentioned above the factor resembled the factor (F1) of Pull man et al. and also that of Andreoli et al. The coupling activity of this factor was cold labile, and somewhat stabilized by the addition of ATP and Mn2+ (Mg2+). These properties also resembled those of the above two factors. However, the present factor had no ATPase activity contrary to the above two factors.
    4. The absence of Mg2+ and Mn2+ during sonic oscillation of mitochondria produced the coupling factor with an ATPase activity suggesting that the present factor without ATPase activity was due to the effect of the metal ion.
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  • Inhibition of Protein Synthesis by Blasticidin S
    II. Studies on the Site of Action in E. coli Polypeptide Synthesizing Systems
    HIDEYO YAMAGUCHI, NOBUO TANAKA
    1966 Volume 60 Issue 6 Pages 632-642
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    Blasticidin S, an aminoacyl-nucleosidic antibiotic, strongly inhibits amino acid polymerization directed by several synthetic polynucleotides to almost the equal extent. So far as examined, no related compounds produce significant inhibition of polypeptide synthesis. The blasticidin S inhibition is markedly reversed with increased concentrations of sRNA and slightly with ribosomes, but no competition is observed with higher concentrations of poly U. Ribosomes precharged with poly U are as sensitive as ribosomes treated with the antibiotic prior to the addition of poly U to the blasticidin S inhibition. The template polynucleotide-directed binding of aminoacyl-sRNA to ribosomes is not affected by high concentrations of blasticidin S. The antibiotic markedly interferes with the puromycin-dependent polypeptide release from ribosomes. From these results it is suggested that blasticidin S acts on the step of peptide transfer from peptidyl-sRNA to incoming aminoacyl-sRNA, without effect on the preceding steps of protein biosynthesis.
    We wish to thank Prof. H. Yonehara for supplying us with blasticidin S and related compounds. This investigation was supported in whole by Public Health Research Grant CA 05082-06, from the U. S. National Cancer Institute.
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  • Studies on the Chemical Nature of Bovine Bradykininogen: Determinations of Amino Acid, Carbohydrate, Amino and Carboxyl Terminal Residues
    SHIGEHARU NAGASAWA, YUKIO MIZUSHIMA, TADASHI SATO, SADAAKI IWANAGA, TO ...
    1966 Volume 60 Issue 6 Pages 643-652
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    Bradykininogen prepared by the methods previously described has been further purified by chromatography on DEAE-Sephadex A-50 and gel-filtration on Sephadex G-200.
    The purified bradykininogen was homogeneous as judged by electrophoretic and ultracentrifugal analyses, and its sedimentation coefficient was calculated to be 2.65 S.
    The polypeptide content of bradykininogen was 72 per cent and its carbohydrate content was 18 per cent, which consisted of 6.0 per cent of glucosamine, 4.4 per cent of galactose, 2, 3 per cent of mannose and 5.3 per cent of sialic acid. All of the sialic acid was released by the action of bacterial neuraminidase. The polypeptide moiety consisted of 40 basic, 79 acidic, 51 aliphatic hydroxyl, 117 aliphatic, 24 aromatic amino acid residues, 25 proline, 13 half-cystine, 4 tryptophan and 3 methionine residues.
    The molecular weight of bradykininogen was calculated to be 49, 500.
    The N-terminal amino acid of bradykininogen was serine and the C-terminal amino acid was leucine. The full biological activity of bradykininogen was retained even after the treatment with carboxypeptidases A and B or leucine aminopeptidase.
    We are indebted to Mr. K. Horiuchi and Miss T. Hattori in this laboratory for their valuable technical assistance.
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  • Analysis of the Acid-soluble Deoxyribosidic Compounds Accumulated in Mitomycin C Treated Bacteria
    ISAMU MATSUMOTO, MAKIKO KOZAKA, YASUYUKI TAKAGI
    1966 Volume 60 Issue 6 Pages 653-659
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    1. The effect of mitomycin C on the bacterial DNA synthesis was studied with an auxotroph, thymine-requiring Escherichia coli B3, by the use of thymine-C14 as a tracer. Treatment of the bacterial cells with proper concentrations of mitomycin C resulted in a greatly reduced rate of DNA synthesis, and a slight but significant degradation of existing DNA.
    2. The amount of acid-soluble deoxyribo-sidic compounds in the cells subjected to mitomycin C treatment was higher than that in the untreated control culture. The major portion of them was newly synthesized compounds of nucleotide form.
    3. Chromatographic profiles of total nu-cleotides and the relative amounts of various compounds in the organism exposed to mitomycin C were almost the same as those in unexposed cells. Treatment of cells with the antibiotic, therefore, leads to an alteration of each nucleotide in quantity, but not in quality.
    4. It was suggested that the degradation of DNA in the cells treated with mitomycin C is not necessarily involved in the events lead-ing to the inhibition of DNA synthesis.
    The research reported here was made possible by the support and sponsorship of the U. S. Department of the Army through its Far East Research Office (DA-92-557-F E C-34525).
    We wish to express our appreciation to Dr. M. Sekiguchi for his helpful suggestions and stimulating discussions.
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  • Studies on P-450
    II. On the Absorption Spectrum of P-450 in Mitochondrial Fragments from Bovine Adrenal Cortex
    SHIGEO HORIE, TADATOSHI KINOSHITA, NORIO SHIMAZONO
    1966 Volume 60 Issue 6 Pages 660-673
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    The absorption spectrum of the sonicated mitochondrial fragments from bovine adrenal cortex was obtained using, as a reference of spectrophotometry, the same preparation which had been denatured with alkali and treated with hydrogen peroxide. Furthermore, the spectrum of the preparation, which had been subjected to a prolonged aerobic treatment with p-chloromercuribenzoate, was subtracted from the corresponding spectrum of the untreated control. The resulting spectrum was assumed to be, at least, very close to that of P-450. The opal glass transmission method was adopted in these Spec trophotometric estimations. Besides P-450, small amounts of cytochrome oxidase and cytochromes b and c1 were present in the preparation. In addition to these, data indicating the presence of a hemopro_??_ein, which was tentatively named R-423, were obtained. The nature of the prosthetic group of P-450 was discussed.
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  • A Study on the Mechanism of Superprecipitation of Myosin B
    TOSHIO MATSUNAGA, HARUHIKO NODA
    1966 Volume 60 Issue 6 Pages 674-681
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    1. The process of superprecipitation of myosin B was studied by measuring the turbidity. Using the stopped flow method with the rapid flow apparatus, it was made clear that the clear phase which was revealed as macroscopical decrease of turbidity did not necessarily precede the onset of superprecipitation.
    2. Superprecipitation was investigated while keeping the ATP concentration constant during the reaction. At a low ATP concentration, the reaction rate showed essentially a first-order dependence on myosin B concentration. The reaction rate was proportional to ATP concentration and did not depend on ionic strength. At the ATP concentration in the neighborhood of 0.1mM, the reaction lingered for a while at an intermediate stage of incomplete superprecipitation. The reaction mixture in this intermediate stage showed a strong flow birefringence. The turbidity and birefringence of the intermediate stage were functions of ATP concentration, while the extinction angle remained constant. Relative extent of superprecipitation of the intermediate state calculated on the basis of flow birefringence was equal to that calculated on the basis of turbidity.
    3. The process of superprecipitation was discussed. It was suggested that the local dissociation of myosin B precedes superprecipitation.
    We wish to express our gratitude to Drs. T. Nakamura and Y. Ogura for allowing us to use their rapid flow apparatus. We are grateful also to Dr. S. Ebashi for his instructive advice.
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  • Reactive Amino Groups in Baker's Yeast Cytochrome c
    CHIAKI SATO, KOITI TITANI, KOZO NARITA
    1966 Volume 60 Issue 6 Pages 682-690
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    The cysteine residue in baker's yeast cyto-chrome c consisting of 108 amino acid residues was quantitatively substituted with N-ethyl-maleimide without an appreciable decrease of the activity. On incubation of the modified cytochrome with trinitrobenzene sulfonate at 0°C, the N-terminal a-amino group (the -5th position) reacted first and then four lysine residues at the 4th, 89th, 100th and an unknown positions with almost the same reactivities. The activity of the modified cytochrome decreased with the increase of the number of the introduced trinitrophenyl group. Although the participation of the three lysine residues in the activity could not clearly be demonstrated, the sulfhydryl and the α- and s-amino groups of the N-terminal and the above four lysine residues were concluded to be exposed on the surface of the cytochrome molecule.
    The authors express their sincere thanks to Sankyo Co. Ltd., for providing us of baker's yeast cytochrome c and to Dr. K. Wada for the assay of cytochrome oxidase activity of the modified derivatives of the cytochrome c.
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  • Studies on Soluble Cytochromes in Enterobacteriaceae
    IV. Possible Involvement of Cytochrome c-552 in Anaerobic Nitrite Metabolism
    TAKESHI FUJITA, RYO SATO
    1966 Volume 60 Issue 6 Pages 691-700
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    The content of cytochrome c-552 was compared in E. coli cells grown under various growth conditions, especially with reference to nitrogen sources and atmospheric conditions. Biosynthesis of cytochrome c-552 was markedly stimulated anaerobically by the presence of nitrate or nitrite in the medium. Hyponitrite, hydroxylamine, ammonium chloride, and glutamate showed no stimulating effect, though anaerobic growth on these nitrogen sources resulted in the consistent formation of small amounts of cytochrome c-552. Evidence was presented that the true inducer of the synthesis of cytochrome c-552 is nitrite and the induction by nitrate is an indirect effect. The induction by nitrite was not influenced by the coexistence of more reduced forms of nitrogen. Oxygen repressed strongly the synthesis of cytochrome c-552 even in the presence of nitrate or nitrite. E. coli could grow anaerobically utilizing nitrate or nitrite as the sole nitrogen source, but no growth occurred in the same medium under aerobic conditions.
    Cytochrome c-552 in intact cells was reoxidized rapidly by nitrate, nitrite, and hydroxylamine. The reduced cytochrome in the soluble fraction and in purified cytochrome preparation was also reoxidized rapidly by nitrite and hydroxylamine, but not by nitrate. These oxidations of reduced cytochrome were inhibited by cyanide.
    The cells grown anaerobically with nitrite as the nitrogen source showed a much stronger nitrite-reducing activity than those grown with ammonium nitrogen.
    Based on these observations the possibility was discussed that cytochrome c-552 is involved in anaerobic reduction of nitrite.
    The authors are indebted to Dr. H. Kumaoka of Hokkaido University for his assistance in preparing sodium hyponitrite.
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  • On the Active Site of Myosin A-Adenosine Triphosphatase
    VI. Existence of Asparaginyl-prolyl-prolyl-lysine near the Active Site
    HARUHIKO TOKUYAMA, SHUICHIRO KUBO, YUJI TONOMURA
    1966 Volume 60 Issue 6 Pages 701-706
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    The authors have previously found tha two moles of lysine residues in one mole o myosin and H-meromyosin react specificall with TBS, and that S-1, the main componen of Fr-2, prepared from a trypsin digest of myosin, retains the intact active site of myosin-ATPase but contains only one mole of specific lysine per mole of S-1. Therefore, the chemical structures around the lysine residues specific to TBS in myosin, H-meromyosin and Fr-2 were compared.
    TNP-protein was digested with Nagarse (1/20 of the weight of protein) and Pronase-P (1/20 of the weight of protein) and the TNP-peptide mixture was isolated with an IRC-50 column. The TNP-peptide mixture was sepa-rated into six fractions by paper chromato-graphy with n-butanol-tert-amyl alcohol-py-ridine-conc. NH4OH-acetic acid-H2O as solvent. From analysis of fractions II and VI in the six fractions it was demonstrated that about 50 per cent of the TNP-peptides isolated from TNP-Fr-2 was an equimolar mixture of Asp (NH2)-Pro-Pro-TNP-Lys and Pro-Pro-TNP-Lys and that the majority of the rest was TNP-lysine, itself. The yields of Asp (NH2)-Pro-Pro-TNP-Lys from TNP-myosin and TNP-H-meromyosin were smaller than that from TNP-Fr-2. Furthermore, it was shown that Pronase-P can release TNP-lysine from Asp (NH2)-Pro-Pro-TNP-Lys.
    Therefore, it was concluded that the chemical structure around the lysine residue specific to TBS in Fr-2, i.e. the lysine located near the active site, is Asp(NH2)-Pro-Pro-Lys, but H-meromyosin contains another lysine residue specific to TBS, which was suggested to be the one in Ser-TNP-Lys-(Gly, Glu, Ser)-(Gly, Ala).
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  • Studies on Erythrocyte Glycolysis
    IV. Kinetics of Pi32 Incorporation into 2, 3-Diphosphoglycerate and ATP
    SHIGEKI MINAKAMI, CHIYO SUZUKI, HARUHISA YOSHIKAWA
    1966 Volume 60 Issue 6 Pages 707-712
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    1. The time course of the incorporation of radioactive inorganic phosphate into 2, 3-diphosphoglycerate and ATP in steady-state glycolysis of red cells was studied.
    2. The incorporation into diphosphoglycerate had always a distinct lag, whereas that into ATP showed no lag.
    3. The specific activities of P32 in the 2 and 3 positions of diphosphoglycerate were the same for the incubation time from 5 to 40 minutes.
    4. In acidic pH, the incorporation into diphosphoglycerate was low and increased with the increase of pH. The incorporation into ATP did not depend so much on pH.
    5. The incorporation of radioactive inorganic phosphate into 2, 3-diphosphoglycerate may possibly be interpreted as due to the exchange reaction in the phosphoglyceromutase step, without considering the contribution of the diphosphoglycerate cycle.
    The authors express their thanks to Miss N. Shinohara for her assistance and to Dr. T. Saito for his discussion. Thanks are also due to Dr. M. Miyamoto, the president of the Plasma Institute, Tokyo, for the generous supply of blood and to Hoansha Foundation for the financial aid.
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  • Proteinase Formation in Relation to Physiological Activities of Growing Mycelia of Aspergillus niger
    HIROBUMI OHAMA, GOTARO TOMONAGA, TOMOMICHI YANAGITA
    1966 Volume 60 Issue 6 Pages 713-717
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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    Aspergillus niger strain 1617 was grown starting from conidia of a relatively large inoculum size, and investigations were made of the changes in activities of some exo- and endo-enzymes and in the rate of S35-incorporation into protein during the course of hyphal development, According to the phases of hyphal growth, characteristic change was observed for each activity measured. The most characteristic was an abrupt decrease in the rate of S35-sulfate incorporation into cellular protein, which was observed just after the sprouting of rudimentary hyphae. The formations of intracellular acid phosphatase was found to follow a similar course to that of extracellular proteinase. The acid proteinase formed at the actively growing phase was observed to be chromatographically different from that formed after the cessation of growth.
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  • Changes in Activities of Serum Aminopeptidase A and Leucine Aminopeptidases of Rats at Various Stages of Growth
    IKUKO NAGATSU, JUN HARA
    1966 Volume 60 Issue 6 Pages 718-720
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Effect of Adenine on the Photodynamic Inactivation of Yeast Alcohol Dehydrogenase in the Presence of Riboflavin
    KIHACHIRO UEHARA, MORIO YONEZAWA, SABURO HOSOMI, RYOJI HAYASHI
    1966 Volume 60 Issue 6 Pages 721-722
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Suppression of Cholesterol Synthesis in Rat Liver by Dihydrocholesterol Administration
    HISASHI TAKIGUCHI, HIROMI NAGATA, JIRO KANNO
    1966 Volume 60 Issue 6 Pages 723-725
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Phosvitin of the Trout Roe
    YUKI ITO, TATSUZO FUJII, MASAKO KANAMORI, TAKAO HATTORI, RYOSAKU YOSHI ...
    1966 Volume 60 Issue 6 Pages 726-728
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Phosphoenolpyruvate Carboxykinase from Rhodopseudomonas spheroides and Its Possible Role in Light-Stimulation of Glucogenesis
    KOKI UCHIDA, GORO KIKUCHI
    1966 Volume 60 Issue 6 Pages 729-732
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Native Tropomyosin-like Action of Troponin on Trypsin-treated Myosin B
    SETSURO EBASHI, AYAKO KODAMA
    1966 Volume 60 Issue 6 Pages 733-734
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Biochemical Role of Thiamine Triphosphoric Acid Ester
    TAKASHI YUSA, BUNJI MARUO
    1966 Volume 60 Issue 6 Pages 735-737
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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  • Crystallization of the Semiquinoid Form of D-Amino Acid Oxidase
    KUNIO YAGI, NOBUHIKO SUGIURA
    1966 Volume 60 Issue 6 Pages 738-740
    Published: December 25, 1966
    Released on J-STAGE: November 18, 2008
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