The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Volume 46, Issue 4
Displaying 1-18 of 18 articles from this issue
  • MITUO EBATA
    1959 Volume 46 Issue 4 Pages 397-406
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Hydrolysis products of synthetic linear polymers, both poly-ε-amino-caproyl-DL-alanine and poly-ε-aminocaproyl-L-alanine by the action of trypsin were investigated by paper chromatographic analysis. Small amounts of free alanine and ε-aminocaproic acid together with large amount of dialysable peptides were found as the dialysable hydrolysis products. Sometimes traces of free ε-aminocaproyl-L-alanine could be observed in the case of poly-ε-aminocaproyl-L-alanine. Furthermore, some studies on the substrate specificity of the enzyme were carried out using a number of synthetic substrates related to the polymer, and a possible mode of action of trypsin upon the poly-ε-aminocaproyl-α-alanines was discussed.
    The author wished to express his hearty thanks to Prof. F. Egami of Nagoya University, Prof. J. Noguchi of this university, Dr. R. Sato, Osaka University and to Dr. N. Sakota, Dainippon Zoki Laboratory, for their kind encouragements throughout the course of this work. The author is also grateful to Mr. K. Morita for his technical assistances.
    The expense of this study was defrayed in part by a grant from the Ministry of Education
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  • MITUO EBATA, KENJI MORITA
    1959 Volume 46 Issue 4 Pages 407-416
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    In studies on the action of trypsin to ε-aminocaproyl compounds it has been shown that the peptides, amide or esters of ε-aminocaproic acid can be partly hydrolysed by the enzyme action. It seems that an enzyme which catalyzes the hydrolysis of these compounds is trypsin itself from the ex-amination of the stability, inhibitions of the enzymes responsible. Optimum pH, Km, and proteolytic coefficient k3, were also determined for the hydrolysis. Several w-amino-n-fatty acid (C5-C3) derivatives, ornithine ethyl ester ε-caprolactarn and adipamide, structurally related to ε-aminocaproic acid derivatives, made completely resistance to the hydrolytic action of the enzyme.
    The authors wish to express their hearty thanks to Prof. F. Egami of Nagoya University, Prof. J. Noguchi of this University, and Dr. R. Sato, Osaka University for their kind encouragements throughout the course of this work. The authors are also grateful to Mr. T. Nojiri for his technical assistances.
    The expense of this study was defrayed in part by a grant from the Ministry of Education.
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  • V. ELECTROPHORETIC AND ULTRACENTRIFUGAL INVESTIGATIONS ON THE HOMOGENEITIES AND SOME PROPERTIES OF α- AND β-LIPOVITELLIN
    HIROSHI SUGANO
    1959 Volume 46 Issue 4 Pages 417-424
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Both α- and β-lipovitellin were homogeneous elect rophoretically in the pH range 6.8 to 9.9 and 4.9 to 10.5, respectively, whereas at pH 4.2 both were heterogeneous. Ultracentrifugal analysis at pH 9.8 and μ 0.15 indicated the heterogeneities of both preparations.
    2. From the mobility curve, the isoelectric point of β-lipovitellin was pH 5.9 at an ionic strength of 0.30.
    3. From the variation of mobility of β-lipovitellin with buffer composi-tion, it was pointed out that the divalent anions such as carbonate and sulfate had the binding ability to β-lipovitellin, but not monovalent ions such as ammonium and chloride.
    4. The mobility of β-lipovitellin depended on the inoic strength of buffer. There was a marked decrease in the mobility of β-lipovitellin with increase in ionic strength.
    5. Some informations on the solubility property of β-lipovitellin in the pH range from 4.0 to 10.0 were obtained.
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  • VI. ON THE α-MALTOSIDASE ACTIVITY OF TAKA-AMYLASE A
    SHOJI MATSUBARA, TOKUJI IKENAKA, SHIRO AKABORI
    1959 Volume 46 Issue 4 Pages 425-431
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The hydrolysis by crystalline Taka-amylase A of α-phenylmaltoside and p-nitrophenyl-α-maltoside was confirmed and the maltosidasc activity of Taka-amylase A was found to be an intrinsic property of this enzyme.
    2. The preparation and properties of crystalline α-phenylmaltoside and the synthesis of p-nitrophenyl-α-maltoside were described.
    3. The method of determination of Taka-amylase A activity using α-phenylmaltoside and p-nitrophenyl-α-maltoside was described, and the maltosidase unit was proposed as a new measure of Taka-amylase activity.
    The authors wish to express their gratitude to Mr. A. Tsugita, T. Matshsim a, K. Yamamoto and Miss H. Toda for their helpful advice through this investigation, and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.
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  • X. ON THE REACTION OF REDUCED HEMOGLOBIN WITH ETHYLISOCYANIDE AND THE EFFECT OF UREA ON THIS REACTION
    TARO OKAZAKI, KEIZOO TSUSHIMA
    1959 Volume 46 Issue 4 Pages 433-443
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Sigmoid coefficient in the reaction of reduced hemoglobin with EIC was calculated to be 2.4 from Hill's equation. This result indicates the existence of heme-heme interaction in the reaction of reduced hemoglobin with EIC.
    2. Dissociation constants of heme-linked acid groups of EIC-hemoglobin were assumed to be similar to those of oxyhemoglobin.
    3. In the presence of 6.0 M urea, the heme-heme interaction decreased (n decreased from 2.4 to 1.4), EIC-combining affinity increased and the Bohr effect disappeared.
    In the presence of urea in lower concentrations, the heme-heme in-teraction did not decrease and the EIC-combining affiinity increased slightly.
    4. The Bohr effect disappeared continuously with the increase of urea concentration.
    Some discussions were made on the mechanism of the Bohr effect.
    The authors are indebted to Prof. K. Kaziro for his continuous help and stimulating discussions. The authors also express their gratitude to the Ministry of Education for assistance from the Scientific Research Fund.
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  • SHYOZO WADA
    1959 Volume 46 Issue 4 Pages 445-452
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Three different kinds of acylases, α-lysine acylase, ε-lysine acylase and D-phenylalanine acylase, capable of performing the resolution of acyl-DL-amino acids, are produced by a Pseudomonas species, KT-83, which was previously isolated from soil by Kameda et al. One of these enzymes, ε-lysine acylase, was purified by treatment with ion exchange resin and by fractionation with ammonium sulfate. The purified enzyme does not possess the activity of the α-lysine acylase, but it has a specific activity against Nε-benzoyl-L-lysine, representing about 4, 000-fold purification of the activity in the original extract. The α-lysine acylase has an optimum pH at 7.8 and the ε-lysine acylase at 6.0. The optimum temperature of both the a-and ε-lysine acylase is 37-38°. Among a variety of ions Zn++ at 10-3 M concentration increases the activity of the ε-lysine acylase against N'-benzoyl-DL-lysine. The purified enzyme was shown by electrophoresis to contain two protein fractions.
    The enzyme hydrolyzes asymmetrically Nε acyl-DL-lysine easily, but is unable to hydrolyze Nα, Nε-diacyl-DL-lysine. From these facts, the asym-metrical hydrolysis of Nα Nε-diacyl-DL-lysine by the crude acylase preparation of KT-83 is considered to proceed as follows; Nα, Nε-diacyl-DL-lysine is first hydrolyzed asymmetrically by the α-lysine acylase to Nα-acyl-L-lysine, which is then hydrolyzed to L-lysine by the ε-lysine acylase.
    The author wishes to express their appreciation to Dr. S. Kuwada, Dr. S. Tatsuoka and Dr. Y. Kameda for their great favor and continuous interest.
    Thanks are also due to Dr. E. Ohmura, Mr. A. Miyake and Dr. K. Ogata for their support, and to Mr. I. I mad a and Mr. K. Tomoda for their technical help.
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  • KAZUOKI KURATOMI
    1959 Volume 46 Issue 4 Pages 453-461
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The action of various inhibitors on pyruvic oxidase system, cocar-boxylase, or thiamine was examined. The catalytic action of thiamine derivatives was also studied instead of thiamine in the reaction of acetoin formation.
    2. Thiamine combined with PCMB was detected and analyzed. It could be concluded that PCMB combines with the thiol group of thiamine.
    3. From the experimental results the active center of thiamine or TDP was discussed. It was concluded that -SH, -NH2, and thiazole-N were possibly responsible for their catalytic action.
    The author wishes to express his gratitude to Prof. N. Shimazono and Dr. N. Hosoya for their encouragement and helpful suggestions.
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  • II. THE EXCHANGE REACTION OF CALCIUM
    ATSUSHI OIKAWA
    1959 Volume 46 Issue 4 Pages 463-473
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The firmly bound calcium atom in TAA is able to exchange in solution with free exogenous calcium ions but not with strontium ions.
    2. During repeated crystallization procedure the calcium atom ex-changes not only with calcium but also with strontium and magnesium ions. The exchange rate is greatest with calcium and smallest with magnesium.
    3. The preparations of TAA produced by A. orytae grown in the media containing no added calcium was found to possess a considerable amount of non-dialysable calcium which might have been derived from impurities.
    4. The TAA protein has a strong affinity to calcium, although the bound calcium can be replaced by strontium without loss of the enzymatic activity.
    5. During the acid inactivation of TAA and its reactivation by neutralization, the enzymatic activity and the amount of non-exchangeable calcium show a good parallelism.
    6. A similar relationship was observed between the enzymatic activity and the change in levo-rotatory power or dispersion constant which may be regarded as a measure of denaturation.
    7. The possible role of the essential calcium atom in the maintenance of enzymatic activity of TAA was discussed.
    The author wishes to express his gratitude to Prof. S. Akabori for his kind guidance, and to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”. The author also wishes to thank Otozai Laboratory, Facultfy of Science, Osaka University, for the determination of metals.
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  • AKIRA TSUGITA, TOKUJI IKENAKA, SHIRO AKABORI
    1959 Volume 46 Issue 4 Pages 475-483
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The partial hydrolysates of DNP-Taka-amylase A were investigated.
    2. Two fractions were obtained by using the adsorption chromatography with talk-celite column and with activated carbon.
    Each fraction was further fractionated by countercurrent distribution method combined with celite or silica gel chromatography.
    3. The structure of three peptides were elucidated to be valyl-(lysine, glutamic acid)-aspartic acid, phenylalanyl-aspartic acid and leucyl-aspartyl-tyrosine.
    The authors are grateful to Sankyo Co., Ltd. for supplying them ‘Takadiastase Sankyo’.
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  • I. BIOCHEMICAL EFFECTS OF GAMMA RADIATION ON UREASE
    SHOZO TANAKA, HIROYUKI HATANO, SHIGETAKE GANNO
    1959 Volume 46 Issue 4 Pages 485-493
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. The inactivating mechanism of enzyme by X-ray irradiations proposed by Dale and Barron et al. was reconfirmed with the effect of γ-rays on urease.
    2. Urease is proved to be more sensitive in its aqueous solution than in an air dried state.
    3. Urease in aqueous solutions is found to be protected against γ-ray inactivation by the presence of several substances such as sodium chloride, glycine, ovalbumin, especially reduced glutathione and cysteine.
    4. By small doses of γ-irradiations inactivation of urease is reversibly relieved by the reducing agents, such as reduced glutathione or cysteine. In this case, oxidation of essential sulfhydryl groups in the enzyme molecules by radiation products of water is causative of its inactivation.
    5. Urease is less sensitive against γ-ray at pH at which the enzyme shows its optimal activity.
    6. Larger doses of γ-ray irradiations cause formation of ammonia in urease solutions and consequent irreversible inactivation of the enzyme activity. Inactivation of this type is attributed to chemical changes occurring in the enzyme molecule, such as the radiolytic breakdown of peptide bonds followed by the oxidative deamination of its component amino acids.
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  • AKIO MAEDA, ATSUSHI OIKAWA
    1959 Volume 46 Issue 4 Pages 495-498
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. Rotatory dispersion of native, dialysed, EDTA-treated and ureadenatured TAA was measured.
    2. Native TAA has an unusually high λc value as compared with other proteins.
    3. The role of calcium was discussed based on the rotatory behavior of TAA.
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  • I. FRACTIONATION OF WAX D OF BCG: ISOLATION OF CORD FACTOR AND OLIGOMANNOINOSITIDES
    SHOSHICHI NOJIMA
    1959 Volume 46 Issue 4 Pages 499-506
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    Wax D of BCG was fractionated into two constituents by silicic acid chromatography. From one fraction, cord factor was isolated and from the other, phosphoinositides containing oligomanno-ose, tentatively designated as “Oligomannoinositides, ” were obtained. The behaviour of “purified wa” on the silicic acid column was discussed.
    The author wishes to thank Dr. D. Mizuno, Chief of the Department of Chemistry, National Institute of Health, Tokyo, for his constant encouragement and advices throughout this work. He is also grateful to Professor Dr. T. Ukita, of the Faculty of Pharmaceutical Sciences, University of Tokyo, for his constant encouragement. Thanks are also due to Miss E. Kondo, of the Department of Chemistry, National Institute of Health, for her skillful technical assistance in every experiment of this work. Micro-analyses for carbon and hydrogen were carried out by Miss S. Hara of the Department of Chemistry, National Institute of Health, Tokyo.
    Addenda: Since this manuscript was submitted it has come to the attention of the author that lipopolysaccharides have been isolated from Wax D of human type strain of tubercle bacilli. They were found in the chloroform eluate from the partition chromato-graphy of wax D on silicic acid. (Personal communication from Dr. Asselineau (Paris))
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  • XXXII. THE PARTIAL SYNTHESIS OF TRIHYDROXY-24-METHYLCOPROSTANIC ACID
    TAKAHIKO HOSHITA
    1959 Volume 46 Issue 4 Pages 507-511
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
    1. 3α, 7α, 12α, -Trihydroxy-24-methylcoprostanic acid was synthesized from norcholylmethyIketone and ethyl DL-α-bromopropionate by modified Reformatsky reaction.
    2. Melting point of methyl 3α, 7α, 12α-trihydroxy-24-methylcoprostanate showed no depression, when mixed with methyl trihydroxyisosterocholanate derived from trihydroxyisosterocholenic acid (this acid was isolated from the bile of Bufo vulgaris formosus)
    . The author wishes to thank Prof. T. Kazuno for valuable suggestions during the course of this work.
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  • MITSUO TORII
    1959 Volume 46 Issue 4 Pages 513-515
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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  • TOSHIO ANDO, FUMIO SAWADA
    1959 Volume 46 Issue 4 Pages 517-519
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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  • AKIHIKO HATTORI, YOSHIHIKO FUJITA
    1959 Volume 46 Issue 4 Pages 521-524
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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  • MASAMICHI KUSUNOSE, EMI KUSUNOSE, YOSHIO KOWA, YUICHI YAMAMURA
    1959 Volume 46 Issue 4 Pages 525-527
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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  • KAZUO YAMADA
    1959 Volume 46 Issue 4 Pages 529-533
    Published: April 25, 1959
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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