The Journal of Biochemistry
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Print ISSN : 0021-924X
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Volume 55, Issue 2
Displaying 1-26 of 26 articles from this issue
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  • On the Mode of Action of Aspergillus ochraceus Proteinase on Oxidized Insulin
    TADAAKI KISHIDA, SADAHIKO YOSHIMURA
    1964 Volume 55 Issue 2 Pages 95-101
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    The oxidized A-and B-chains of bovine insulin were hydrolyzed with crystalline Asp. ochraceus proteinase and the resulting peptides or amino acids in each hydrolysate were qualitatively determined after their separa-tion by column chromatography.
    The proteinase, like those from fungal sources, have rather a broader specificity in its action than pepsin, trypsin, or chrymotryp-sin. The enzyme hydrolyzed the B-chain far more deeper than the A-chain. The clea-vage in the above peptides occurred rapidly at such bonds, where glutamic acid, leucine, tyrosine, valine, or serine is linked by its re-spective carboxyl group, and slower at the carboxyl side of cysteic acid, glutamine, or asparagine.
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  • Association and Dissociation of Bacillus subtilis α-Amylase Molecule
    II. Studies on Monomer-Dimer Transformation by Gel Filtration
    KINJI KAKIUCHI, SUSUMU KATO, AKIRA IMANISHI, TOSHIZO ISEMURA
    1964 Volume 55 Issue 2 Pages 102-109
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1) The studies on monomer-dimer trans-formation of Bacillus subtilis α-amylase mole-cule were made by measuring the sedimen-tation velocities as well as by the dextran gel filtration (Sephadex G-100). The results obtained in either case was the same and the following scheme: 2 Monomer +Zn2+_??_Dimer, is hold in the present experimental conditions.
    2) The elution diagrams and the sedi-mentation patterns were varied with the concentration of B. α-amylase, that is, at the high concentration the faster moving com-ponent corresponded to dimer form, 6.2S, whereas the slower moving component mono-mer form, 4.4 S. At the lower concentration only a single peak was observed.
    3) The following conclusion was deduced from the elution diagrams varied with the elution rate and the quantitative analysis of zinc ion contained in the effluent. The rate of the equilibration between monomer and dimer was equal to the flow rate of the gel filtration in the present experimental con-ditions.
    4) The ultracentrifugal experiments were carried out in the wide range of the concentration of B. α-amylase. At the concen-tration of less than 0.1 per cent s20w dec-reased sharply from 6. 2 S to 4. 4 S and also the sedimentation patterns showed a single peak.
    5) As evidenced from the present investi-gation the enzyme should be in the mono-mer form under the experimental conditions assaying the enzymatic activity. As can be seen in Table II, the enzymatic activity was unchanged in the presence of high concen-tration of zinc ion. Accordingly, it might not be affected by the change of monomer-dimer transformation. The authors would like to express their thanks to Daiwa Kasei Co., Ltd. for supplying Bacillus subtilis α-amylase.
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  • Effect of Temperature and Potassium Chloride Concentration on the Onset of Superprecipitation of Actomyosin Adenosinetriphosphatase Studies
    KOSCAK MARUYAMA, YAYOI ISHIKAWA
    1964 Volume 55 Issue 2 Pages 110-115
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    When the temperature was lowered, the KCl concentration where superprecipitation of actomyosin just sets in became smaller; at 0°C the critical KCl concentration was 0.035M (_??_/2_??_0.06) at pH 7.2 in the presence of 1mM ATP and MgCl2. Above that KCl concentration, clearing response occurred. The actomyosin ATPase activity changed in close relation to its colloidal state, depending upon temperature and KCl concentration. Chelating agents were effective in causing clearing response of actomyosin at low tem-perature and low ionic strength and Ca_??_reversed the action of the chelating agents to induce the onset of superprecipitation.
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  • Fractionation of the Vegetative Pool Deoxyribonucleic Acid of Bacteriophage T2 by the Methylated Bovine Serum Albumin Column
    YUKITO MASAMUNE
    1964 Volume 55 Issue 2 Pages 116-121
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    The DNA of the cells infected with bacteriophage T2 was extracted with phenol and fractionated by the methylated bovine serum albumin column. It was indicated that the pool-DNA was chromatographically different from DNA of mature phage. Ad-dition of chloramphenicol blocked the trans-formation of vegetative DNA to a mature state.
    The author wishes to express his gratitude to Prof. D. Mizuno, Dr. J. Tornizawa, Dr. H. Saito and Dr. K. Miura for the helpful discussions and advices.
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  • Incorporation of O18 from Air into Tyrosine
    KIKUKO TAKASHIMA, DAISABURO FUJIMOTO, NOBUO TAMIYA
    1964 Volume 55 Issue 2 Pages 122-125
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    The incorporation of atmospheric oxygen into the hydroxyl group of tyrosine by Pseudomonas aeruginosa cells, by rat liver prepara-tion and by silkworms was confirmed with O18 as a tracer.
    The authors are grateful to Dr. T. Fukuda of the Sericultural Experiment Station for helpful advice and for a gift of silkworms. The authors are also indebted to Mr. Y. Takashima for his assistance.
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  • Biosynthesis of Myo-Inositol in Rat Seminal Vesicles and Prostates
    YOH IMAI
    1964 Volume 55 Issue 2 Pages 126-130
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. Myo-Inositol was biosynthesized in slices of seminal vericles and prostates of the rat from differently labeled glucoses. Signifi-cant relationship was not recognized between the relative incorporation of radiocarbon into inositol and the labeled position of substrate glucoses, suggesting that an intact glucose moiety contributes to myo-inositol.
    2. C14-Distribution pattern in synthesized inositol, determined through D-and L-idaric acid as well as through myo-inosose-2, also strongly suggested that glucose serves as a precursor for inositol without the molecular partition.
    The early part of the work was carried out with Dr. Frank Eisenberg, Jr., at the Laboratory of Bio-chemistry and Metabolism, National Institute of Art-hritis and Metabolic Diseases, Bethesda, U.S.A., under the direction of Dr. DeWitt Stetten, Jr., with excellent technical assistance of Mrs. Harriet Petropoulos, sup-ported with the Damon Runyon Research Fund.
    The work has been continued under the encour-agement of Prof. Morio Yasuda of this department and supported with the Tokyo Biochemistry Research Society.
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  • Oxidative Phosphorylation Coupled with Nitrate Respiration
    II. Phosphorylation Coupled with Anaerobic Nitrate Reduction in a Cell-Free Extract of Escherichia coli
    AKIHIRO OTA, TATEO YAMANAKA, KAZUO OKUNUKI
    1964 Volume 55 Issue 2 Pages 131-135
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    Oxidative phosphorylation coupled with anaerobic nitrate reduction was found to occur in cell-free extracts of Escherichia coli. The P/NO3- ratios during the reduction of nitrate to nitrite were 0.65 and 1.1 with glutamate and citrate, respectively, as electron donors. Phosphorylation coupled with nitrate reduction was inhibited in the presence of KCN and 2, 4-dinitrophenol but not in the presence of CO. Antimycin A and amytal acted as uncouplers of phosphorylation cou-pled with nitrate reduction.
    The authors wish to express their thanks to the Public Health Research Institute of Kobe City, Kobe for its generosity in providing the strain of E. coli used here.
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  • The Base Composition of Fractionated Transfer Ribonucleic Acids from Yeast
    MITSUHIKO TADA, MARIKO TADA, KUNIO YAGI
    1964 Volume 55 Issue 2 Pages 136-141
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. The nucleotide composition of transfer RNA has been determined quantitatively by chromatography with a small column com-bined with spectrophotometry and fluoro-metry.
    2. Fluorometric assays for thymidylic acid, 5-methylcytidylic acid and two methyl-ated guanylic acids made it possible to analyse the minor components in transfer RNA.
    3. Transfer RNAs fractionated by a countercurrent distribution was analysed for their base compositions. It was revealed that the valine specific transfer RNA rich fraction contained much cytidylic acid and 5-ribosyl-uridylic acid and less uridylic acid and adenylic acid than the serine specific transfer RNA rich fraction.
    The authors are indebted to the Inuyama Plant of Toyo Spinning Co., Ltd. for supplying with a raw material of RNA of Torula yeast.
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  • Metabolism of Drugs
    XL. Enzymatic Oxidation of Methylhexabital 3. Purification and Properties of 3-Hydroxy-methylhexabital Dehydrogenase
    KEIKO TOKI, HISAO TSUKAMOTO
    1964 Volume 55 Issue 2 Pages 142-147
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. 3-OH-MHB dehydrogenase has been purified about 55-fold from a crude soluble fraction of rabbit liver.
    2. During the course of the purification, 3-OH-MHB dehydrogenase was separated from alcohol dehydrogenase.
    3. Purified 3-OH-MHB dehydrogenase required NAD+ or NADP+ as hydrogen acceptor.
    4. Km value for 3-OH-MHB was 9.6×10-5M with NAD+ and 1.9×10-5M with NADP+ at pH 9.6.
    5. Optimal pH for 3-OH-MHB was 9.5 with NAD+ and 10.6 with NADP+. The maximal rate with NAD+ was about twice as much as that with NADP+.
    6. The purified 3-OH-MHB dehydro-genase was specific for 3-OH-MHB, 3-OH-EHB and cyclohexen-3-ol. But several alco-hols, which were substrates of alcohol dehy-drogenase, glucose and some hydroxy steroids were not dehydrogenated by this dehydro-genase.
    Moreover, the alcoholic derivative of alkyl side-chain of barbiturate, such as (ω-l)-OH-seconal, was not metabolized.
    The authors wish to express our gratitude to Dr. B. B. Brodie, of the National Institutes of Health in U.S.A., for supplying crystalline horse liver alcohol dehydrogenase; to Teikokuzoki Pharmaceutical Go. Ltd. for donation of steroids; to Dr. S. Toki, of Fukuoka University, for his helpful discussion; and to Miss R. Yamasaki for technical assistance in this study.
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  • Some Properties of Hemoglobin of Anadara Inflata
    NOBUKO SUMITA, AKIHIKO KAJITA, KOOZOO KAZIRO
    1964 Volume 55 Issue 2 Pages 148-153
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    Crystalline hemoglobin from anadara inflata shows the heme-heme interaction coef-ficient of 1.7 and no Bohr effect when ethyl isocyanide is used as ligand. Although the pigment has six reactive sulfhydryl groups, PCMB does not exhibit any effect on the heme-heme interaction.
    Anadara hemoglobin is less stable to alkali denaturation and much more autoxidizable in the presence of sodium benzoate than horse hemoglobin. The heme groups of the former are dissociable from the protein more easily than the latter.
    Oxidation of anadara hemoglobin by fer-ricyanide results in the formation of hemi-chrome instead of methemoglobin.
    Peroxidase- and oxidase-activities of this hemoglobin were also studied in comparison with those of horse hemoglobin.
    The authors wish to express their appreciation to Mrs. K. Sato, the Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, for her kind advice in the preparation of crystalline hemoglobin from anadara inflata. This work was supported by a Grant for Scientific Research from the Ministry of Education.
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  • Hemoglobins from Erythrocytes of Eel, Anguilla japonica
    KINZABURO HAMADA, NOBUKO SUMITA, TARO OKAZAKI, RYOITI SHUKUYA, KOOZOO ...
    1964 Volume 55 Issue 2 Pages 154-162
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. Two distinct hemoglobins were chro-matographically separated from red cells of Anguilla japonica.
    2. From the sedimentation and diffusion measurements, the molecular weight was determined to be 65, 200 for one (named E1) of these hemoglobins and to be 68, 800 for the other (named E2)
    . 3. The isoelectric point of E1 was to be 8.08 and of E2, 5.96.
    4. Absorbancy maxima of the deriva-tives of these hemoglobins are presented.
    5. Twelve sulfhydryl groups were found in one mole of E2, while none in E1.
    6. One mole of both hemoglobins con-tains four moles of protoheme.
    7. Tyrosine and tryptophan contents and finger print maps indicated that these hemoglobins may differ from each other in primary structure.
    8. E1 was more resistant than E2 to alkali-denaturation and to autoxidation in the presence of benzoate.
    9. As tested with ethyl isocyanide, Et exhibited the same order of the heme-heme interaction with that of horse hemoglobin, but much less interaction in E2, and both hemoglobins completely lacked the Bohr effect.
    The authors wish to express their appreciation to Miss M. Takahashi, Department of Physiological Chemistry, Faculty of Pharmaceutical Science, Univer-sity of Tokyo, for the performance of ultracentrifugal analysis.
    This work was supported by a Grant for Scien-tific Research from the Ministry of Education.
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  • Role of the Hypothalamus in the Induction of Tryptophan Pyrrolase Activity in Rabbit Liver
    TAKASHI SHIMAZU
    1964 Volume 55 Issue 2 Pages 163-171
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. Induction of tryptophan pyrrolase activity of rabbit liver by hypothalamic lesion or stimulation was studied.
    2. When the sympathetic area of the hypothalamus was bilaterally destroyed, tryptophan pyrrolase activity of liver homo-genates increased to about three times the normal value 1 day after the destruction, and returned to the normal level 3 to 6 days after the destruction. Bilateral hypothalamic lesions of the parasympathetic area had little influence on the activity. An increase in activity of liver homogenates of about 8 fold was observed after electric stimulation of the sympathetic area of the hypothalamus. An increase of nearly 5 fold in activity of liver homogenates was also observed after electric stimulation of the parasympathetic area of the hypothalamus.
    3. Electrical stimulation of the sympa-thetic area resulted in a marked elevation of the total tryptophan pyrrolase activity and one-half of this enzyme was saturated with respect to its cofactor, in vivo. When the parasympathetic area of the hypothalamus was stimulated, the total amount of enzyme also increased markedly but only one-fifth of this enzyme was combined with cofactor.
    4. The induction of enzyme activity by hypothalamic stimulation was also observed in an adrenalectomized rabbit.
    5. These studies indicate that two fur-ther influences, namely the sympathetic and parasympathetic areas of the hypothalamus, are involved in the induction of tryptophan pyrrolase activity in mammalian liver.
    The author wishes to thank Professors T. Ban, M. Suda, and Y. Sakamoto for their advice and encouragement. Thanks are also due to Dr. A. Takakusu for his valuable suggestions.
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  • Bau eines Dreistrahlenspektrophotometers
    TSUYOSHI OHNISHI
    1964 Volume 55 Issue 2 Pages 172-177
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. Durch eine weiterentwickelte Anwendung der Eigenschaften eines Systems von Rotativsektoren und elektronischen Schaltungsschlüssen war es möglich, ein bisher noch nicht existierendes Dreistrahlenspektrophotometer (triple-beam spectrophotometer) zu bauen, mit dem die Veränderungsunterschiede der optischen Dichte an drei Wellenlängen gleichzeitig gemessen werden konnen.
    2. Das neuerdachte Dreistrahlenspektrophotometer besitzt folgende Eigenschaften: Die Geräusche während der Registrierung des Unterschieds der optischen Dichte für eine Reaktionszeit (10-90%) von einer Sekunde können auf 3×10-4 herabgesetzt werden, (ii) die Abweichung während einer einstündigen Registrierung der optischer Dichte kann auf 10-3, und (iii) die Interferenz zwischen je einem Strahl entsprechenden Stromkreisen unter 0.1 Prozent gehalten werden.
    3. Als Messungsbeispiele wurde das Dreistrahlenspektrophotometer in zwei Fällen angewendet, im erstens, zur gleichzeitigen Messung der Veränderungen der Cytochrompigmente in der Mitochondrien and der dabei auftretenden Trübungsveränderung der Mitochondrienlösung, und im zweiten, zur Messung der momentanen, durch ATP hervorgerufenen Ca-lonen Verbindung mit den Muskelgrana und der debei auftretenden Trübungsveränderung des Muskelgranalösung.
    Aufrichtiger Dank für Ratschläge und Hilfe sei Herrn Professor Dr. B. Hagihara der Medizinischen Fakultät der Universität Osaka, und Herrn K. Miwa der Wissenschaftlichen Fakultät der Universität Nagoya, für stets bereitwillige Mitarbeit ausgedruckt.
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  • Purification and Chemical Characterization of the Specific Antigenic Protein of Rat Ascites Hepatoma Cells
    HIDEMATSU HIRAI, HIROKO TAGA, KOTARO WARABIOKA
    1964 Volume 55 Issue 2 Pages 178-184
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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    The specific antigenic protein in the pH 4.8 extract of Yoshida's rat ascites hepatoma cells (AH49 strain) or of their nuclear fraction was partially purified by ion exchange cellu-lose chromatography.
    The amount of the protein obtained was about 0.1% of total protein of the cancer cells.
    Chemical analyses indicated that the protein contained all of the common amino acids and was rich in acidic amino acids qualitatively but contained no appreciable amount of carbohydrates, nucleic acids or lipids.
    The protein was very soluble in water and migrated in the electric field with the mobility of serum α-globulin at pH 8. The solubility of the purified protein was that of euglobulin. The purified protein gave specific precipitin bands with rabbit antisera against the pH 4.8 extract of the cancer cells.
    The authors express their deep appreciation to Professor Norio Shimazono, Department of Biochemis-try, Faculty of Medicine, University of Tokyo, Tokyo, and to Dr. Tomizo Yoshida, Head, Cancer Institute, Japanese Foundation for Cancer Research, Tokyo, for their interest in this study. The authors also thank Dr. Heinz Specht, Chief, Pacific Office, NIH, U.S.A. for his suggestions concerning the preparation of this manuscript.
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  • The Gelation of Ovalbumin Solution by High Pressure
    CHIEKO SUZUKI, KEIZO SUZUKI
    1964 Volume 55 Issue 2 Pages 185-187
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Exchange Reaction of Ethyl Isocyanide and Oxygen in Oxyhemoglobin
    NOBUKO SUMITA, TARO OKAZAKI, RYOITI SHUKUYA, KOOZOO KAZIRO
    1964 Volume 55 Issue 2 Pages 188-191
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Cardiac Myosin B and Calcium Ions
    MASANORI OTSUKA, FUMIKO EBASHI, SHOIGHI IMAI
    1964 Volume 55 Issue 2 Pages 192-194
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Effect of p-Chloromercuribenzoate on Tryptophan Peroxidase of Normal Rat Liver In Vitro
    KATSURO KOIKE, SEIICHI OKUI
    1964 Volume 55 Issue 2 Pages 195-196
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Flavin Content of D-Aminoacid Oxidase
    KUNIO YAGI, TAKAYUKI OZAWA
    1964 Volume 55 Issue 2 Pages 197-198
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Transaminase Activities in Some Rapidly Growing Tissues
    YOZO NAKATA, TOSHIHIKO SUEMATSU, YUKIYA SAKAMOTO
    1964 Volume 55 Issue 2 Pages 199-201
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • The Chemical Structure of Human Kidney Globosibe
    AKIRA MAKITA, MICHIKO IWANAGA, TAMIO YAMAKAWA
    1964 Volume 55 Issue 2 Pages 202-204
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • A Rapid Permethylation of Glycolipid, and Polysaccharide Catalyzed by Methylsulfinyl Carbanion in Dimethyl Sulfoxide
    SEN-ITIROH HAKOMORI
    1964 Volume 55 Issue 2 Pages 205-208
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Purification and Characterization of Two Types of Cellulase from Trichoderma koningi
    TERUO IWASAKI, KATSUYA HAYASHI, MASARU FUNATSU
    1964 Volume 55 Issue 2 Pages 209-212
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • Fingerprint Maps and NH2-Terminal Amino Acids of Bullfrog and Tadpole (Rana catesbeiana) Hemoglobins
    KINZABURO HAMADA, RYOITI SHUKUYA, KOOZOO KAZIRO
    1964 Volume 55 Issue 2 Pages 213-214
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • The Fatty Liver Induction by α-Ethylthioisonicotinamide (Ethioniamide, 1314th)
    FUMIO ITO, YUICHI YAMAMURA, KAZUO HAYANO
    1964 Volume 55 Issue 2 Pages 215-216
    Published: February 25, 1964
    Released on J-STAGE: November 18, 2008
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  • ERRATA for Vol.54 (July-December, 1963)
    1964 Volume 55 Issue 2 Pages e1-e2
    Published: 1964
    Released on J-STAGE: November 18, 2008
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