The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
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Volume 56, Issue 2
Displaying 1-14 of 14 articles from this issue
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  • On the Carbon Monoxide-Shift of Absorption Spectrum of Cytochrome a3
    SHIGEO HORIE
    1964Volume 56Issue 2 Pages 113-121
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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    The difference spectra (carbon monoxide compound minus reduced compound) of various heme compounds were compared. It was found that the difference spectra could be classified into two types. Cytochrome a3, peroxidases, and hemoglobins belonged to one type (type I), and denatured cytochrome a, denatured cytochrome c, hemochromes, and hemoprotein cyanide complexes belonged to the other type (type II). The type II pattern was essentially the mirror image of the type I pattern. The different 6-coordination states of the reduced compounds were assumed to be the cause for the difference between these types of spectra. Therefore, the carbon monoxide shift of cytochrome a3 is not neces-sarily a unique shift among the natural CO-binding hemoproteins. Cytochrome o idase treated with sodium dodecyl sulfate showed the shift, the type of which was different from that of cytochrome a3.
    The author expreses his cordial thanks to Prof. N. Shimazono for his kind advice and encourage-ment. The author wishes also to send his heartful thanks to Dr. M. Morrison of the City of Hope Medical Research Institute for his kind support and advice.
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  • Isolation and Analysis of Multiple Forms of Caeruloplasmin
    TOSHIO KAYA
    1964Volume 56Issue 2 Pages 122-127
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    Porcine caeruloplasmin was separated into more than two components which are different with their physico-chemical properties and chemical compositions. Bovine caeruloplasmin was also separated in two components. Cry-stalline human caeruloplasmin obtained by the procedure according to Deutsch was further purified. The sugar content and the value of E279/E610 for the purified sample were found to be smaller than those before pirifi-cation.
    The author wishes to express his deep gratitude to Prof. T. Sato and Dr. J. Yoshimura, Tokyo In-stitute of Technology, for their kind guidances thr-oughout this investigation, and also thanks Mr. H. Mukasa and Mr. T. Takamoto for their help in tar-ring out the experiments.
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  • The Activation of α-Chymotrypsinogen with Proteinase of Streptomyces griseus
    HIROSHI HASHIZUME, KAZUTOMO IMAHORI
    1964Volume 56Issue 2 Pages 128-137
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    It was found that proteinase produced by Str. griseus can activate α-chymotrypsinogen. The enzyme which was activated by a limited proteolysis with Str. proteinase, in the pres-ence of β-phenylpropionate was homogeneous on column chromatography, centrifugal sedi-mentation pattern and paper electrophoresis. This enzyme is called σ-chymotrypsin. Sigma-chymotrypsin has almost the same enzymatic properties (specific activity, Km, Ki) as these of π-chymotrypsin and is quite similar in the secondary and tertiary structure. N-terminal and C-terminal amino acids of o-chymotrypsin were examined and it was found N-terminal amino acid is isoleucine. Both lysine and arginine were found to be C-terminal amino acids. It was suggested that o-chymotrypsin is not homogeneous and the activation mechanism with Str. proteinase is somewhat different from that of tryptic activation. A schema of Str. proteinase activation is pro-posed and the activation mechanism is dis-cussed.
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  • Purification and Properties of Uridine Diphosphoglucose 4-epimerase from Escherichia coli
    YASUO IMAE, NOBUKO MORIKAWA, KIYOSHI KURAHASHI
    1964Volume 56Issue 2 Pages 138-144
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    A method for purification of UDPglucose 4-epimerase from Escherichia coli was described. An overall purification of 80-fold above the crude extract was achieved.
    With the use of this partially purified enzyme preparation, some of its properties were studied.
    The Km value is 1.6×10-4M for UDP-galactose and 1.0×l0-3M for UDPglucose. The enzyme has a broad pH optimum between 7.5 and 9.0. This enzyme does not require a catalytic amount of NAD for its reaction, and the enzyme activity is not inhibited by p-chloromercuribenzoate.
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  • Isolation of Uridine Diphosphogalactose from Escherichia coli Mutant Cells
    NOBUKO MORIKAWA, YASUO IMAE, HIROSHI NIKAIDO
    1964Volume 56Issue 2 Pages 145-150
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    An improved method for the isolation of UDPgalactose from a mutant of Escherichia coli is described. The purity of the prepara-tion is about 95% when it is measured enzy-matically and spectrophotometrically and the yield is 13μmoles per liter of culture.
    The authors are indebted to Drs. K. Kurahashi and T. Fukasawa for helpful suggestions and discus-sions made during the course of this work.
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  • Inhibitory Action of Trialkyltin Compounds on Oxidative Phosphorylation in Mitochondria
    NOBUHITO SONE, BUNJI HAGIHARA
    1964Volume 56Issue 2 Pages 151-156
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    1. Trialkyltin compounds inhibited the mitochondrial respiration stimulated by ADP and the synthesis of ATP but affected little the state 4 respiration.
    2. Tri-n-butyltin chloride inhibited Pi32-ATP exchange reaction and DNP-induced ATPase activity to the same extent as the inhibition to oxidative phosphorylation.
    3. Inhibitory potency of trialkyltin de-rivatives to the phosphorylating respiration was compared.
    4. A stoichiometric inhibitory pattern between TBTC and mitochondria was de-monstrated.
    5. TBTC did not inhibit the DNP-stimulated respiration at the concentration which was sufficient to the inhibition to the phosphorylating respiration.
    6. From the above results, the mecha-nisms of action of trialkyltins were discussed.
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  • The Stimulation of the Pentose Phosphate Pathway in Ascites Tumor Cells by Triphenyltetrazolium Chloride
    SHOJIRO SATO, KIYOMI SATO
    1964Volume 56Issue 2 Pages 157-171
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    The stimultson of the pentose phosphate pathway in Ehrlich ascites tumor cells by 2, 3, 5-triphenyltetrazolium chlordide (TTC) was investigated in comparison with that by methylene blue (MB).
    1. Evidence was presented that TTC at high concentrations stimulated the pentose phosphate pathway.
    2. The mode of action of TTC was compared with that of MB. It was found that, as a whole, both dyes behaved similarly I. in stimulating glucose respiration and respiratory C14O2 output from C14-labeled glucose, 2. in bringing about the high pro-portion of the total oxygen consumed accoun-table for by the oxidation of glucose, 3. in reversing the inhibition of glucose respiration due to respiratory chain inhibitors such as amytal, antimycin A and cyanide, and 4. in that the stimulated glucose respiration was inhibited by glycolytic inhibitors such as iodoacetate.
    3. The possibility that TTC can act as a reversible oxidation-reduction mediator like MB under certain conditions was suggested and discussed.
    4. The behaviors of glucose carbon 1 and 6 oxidations in the presence of stimula-tors and inhibitors were discussed.
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  • Metabolism of S-Methylmethionine
    I. Bacterial Degradation of S-Methylmethionine
    KAZUKO TANAKA, KEIJI NAKAMURA
    1964Volume 56Issue 2 Pages 172-176
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    The cleavage of S-methylmethionine to dimethyl sulfide and homoserine was demon-strated by soil bacterial cells or its sonic extract. Degradation product, homoserine, was isolated from the reaction mixture in essentially pure state.
    The authors are grateful to Prof. T. Suzuki for his encouragement throughout this work.
    The authors are indebted to Mrs. M. Kamenori for elemental analyses and also to Dr. K. Machida and Mrs. I. Hamanaka for infrared spectral measurements.
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  • Stero-Bile Acids and Bile Sterols
    LXIII. Studies on the Bile of the Family Cyprinidae
    TAKAHIKO HOSHITA, SADAO NAGAYOSHI, MINORU KOUCHI, TARO KAZUNO
    1964Volume 56Issue 2 Pages 177-181
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    The occurence of cholic acid is confirmed in the bile of all species of the family Cypri-nidae examined, the chief constituent of which is cyprinol.
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  • Studies on the Chemical Structure of Colistin
    IV. Chemical Structure of Colistin B
    TOMOJI SUZUKI, KAZUO FUJIKAWA
    1964Volume 56Issue 2 Pages 182-189
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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    The full structure of colistin B was determined as IOA→(α) DAB→-Thr→(α) DAB→(α) cyclo-(γ) DAB→(α) DAB→D-Leu→(α) DAB→(α) DAB→-Thr→with combination of enzymatic digestion and acid partial hydrolysis. The structure is identical to that of colistin A, with the exception that colistin B contains isoöctanoic acid instead of 6-methyl-octanoic acid in colistin A.
    The authors with to thank Mr. T. Yano of Banyu Pharmaceutial Co., Ltd. for a gift of commercial colistin and to express our appreciation to Dr. T. Kawano of Osaka College of Pharmacy for the microbiological analysis.
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  • Interaction of Papain with Anti-Papain
    YOSHIMI OKADA, SHOICHI NAKASHIMA, MASAKAZU ASAHI, YUICHI YAMAMURA
    1964Volume 56Issue 2 Pages 190-191
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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  • The Effects of Ultraviolet Irradiation on Induced Formation of Catechol Oxygenase in Pseudomonas effusa
    JOE ATSUTA, KEIICHI NOZU, HIDEO YAMAGISHI, ICHIJIRO HONJO
    1964Volume 56Issue 2 Pages 192-194
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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  • The Enzymatic Conversion of Phytoene to β-Carotene
    YOSHIKO KAKUTANI, GINZABURO SUZUE, SHOZO TANAKA
    1964Volume 56Issue 2 Pages 195-196
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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  • The Status of Tyrosinase in Smooth-Surfaced Membranes of Melanocyte
    MAKOTO SEIJI, SADAO IWASHITA
    1964Volume 56Issue 2 Pages 197-199
    Published: August 25, 1964
    Released on J-STAGE: November 18, 2008
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