-
I. Glycolipid of Corbicula, Corbicula sandai
TARO HORI, OSAMU ITASAKA, TSUYOSHI HASHIMOTO
1964 Volume 55 Issue 1 Pages
1-10
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The pyridine-soluble lipids from tissue of corbicula afforded four main glycolipids. Purification was carried out by adsorption on activated silica gel and Florisil or by mild alkaline saponification.
Among these glycolipids, from the in-frared spectra and the analytical data or thin layer chromatograms, the one containing fatty acid, sphingosine, D-glucose, D-Xylose, L-fucose, glucosamine and galactosamine, or sometimes a related substance, is considered to be present. Especially, the presence of aminosugar phosphate, as a constituent, is an interesting finding.
The autheres are particularly indebted to Prof. T. Yamakawa of the University of Tokyo for his suggestions and encouragement during this investi-gation. They also express their gratitude to Dr. I. Matsubara of Toyo Rayon Co., Ltd. for the elemental analysis.
View full abstract
-
HITOSHI SHICHI, IKUZO URITANI
1964 Volume 55 Issue 1 Pages
11-18
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The electron transport system of a phytopathogenic fungus,
Ceratocystis fimbriata has been studied. The mycelial respiration of this fungus was completely inhibited by antimycin A. Carbon monoxide also inhi-bited the respiration and the inhibition was reversed by light. The mitochondrion-like particles prepared from the mycelium showed the NADH
2: and succinate; cytochrome c oxidoreductase activities which were highly sensitive to antimycin A.
Reduced cytochrome
c was rapidly oxi-dized by the particles and the cytochrome
c oxidase activity was inhibited by CO and the inhibition was light-reversible. The dif-ference absorption spectra of the particles revealed the presence of a classical cyto-chrome system. From these results it was concluded that a typical cytochrome system functions in this fungus as the terminal oxi-dase system. There was no qualitative dif-ference in electron transport between my-celium and conidium.
Of abnormal metabolites known to accu-mulate in the diseased sweet potato tissue, ipomeamarone was found to inhibit potently NADH
2: cytochrome
c oxidoreductase of the fungal particles. The activity was severely inhibited by amytal at a concentration that inhibits only slightly oxidative phosphory-lation of sweet potato mitochondria.
We are indebted to Dr. H. Imaseki in this laboratory for preparing pure ipomeamarone.
View full abstract
-
TOSHIO OKAMOTO
1964 Volume 55 Issue 1 Pages
19-23
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The species specificity of phenylalanine s-RNA of yeast and
E. coli was examined.
In the activation of phenylalanine, the spe-cificity concerns to aminoacyl-s-RNA syn-thetase and the s-RNA, but transfer enzyme and ribosomes are not specific toward s-RNA and it seems to have the same coding site in these organisms in regard to phenylalanine. A partial purification of phenylalanine s-RNA of yeast was achieved by the combined use of a dye-addition method followed by methy-lated albumin column chromatography.
The anther wish to express the thanks to Dr. M. Takanami for various help, and to Dr. Y. Kawade for his helpful discussions. Thanks are also due to Dr. Y. Kuroiwa of Kirin Research Institute for generous supplies of brewer's yeast. This work was supported in part by grant from the Scientific Research Funds of the Ministry of Education, Japan (No. 95637).
View full abstract
-
IV. Effects of Ethylene Glycol, Polyethylene Glycol and Sucrose on the Physico-chemical and Enzymatic Properties of Muramidase
KOZO HAMAGUCHI, KATSUYA HAYASHI, TAIJI IMOTO, MASARU FUNATSU
1964 Volume 55 Issue 1 Pages
24-29
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The physico-chemical and enzymatic properties of muramidase in aqueous so-lutions of ethylene glycol, polyethylene glycol and sucrose have been examined. Ethylene glycol and polyethylene glycol disrupt neither the helical structure nor the hydrophobic region of the muramidase molecule.
The activity of muramidase does not change in the presence of sucrose or glycerine. However, ethylene glycol, dioxane, dimethyl-sulfoxide, and N, N-dimethylformamide de-crease the activity in the concentration range where no structural change of the molecule can be detected.
The authors are indebted to Prof. T. Isemura for his encouragement. They also wish to thank Dr. T. Takagi for discussions.
View full abstract
-
TERUO IWASAKI, KIYOCHIKA TOKUYASU, MASARU FUNATSU
1964 Volume 55 Issue 1 Pages
30-36
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
1. Glycol Cellulose (GC) was confirmed to be a more favorable substrate than carboxymethylcellulose (CMC) for the assay of cellulase preparation obtained from
Trichoderma koningi, particularly in the vis-cometric method, since the viscosity of its solution was not affected by pH or ionic strength.
2. While there were small differences between the dependence curves of activity on pH and temperature, as obtained by both viscometric and reducing power methods, the optimum pH and temperature of the crude cellulase activity toward GC were found to be equal for the two methods at approximately pH 4.0 and 45-55°C re-spectively.
3. No marked difference was observed between the mode of enzymatic hydrolysis of GC and that of CMC.
4. The rates of decrease in viscosity and increase in reducing power during the hydro-lysis of GC by the crude cellulase prepa-ration were observed to be proportional to the concentration of the enzyme preparation at low concentration ranges.
The authors wish to express their hearty thanks to Dr. R. Senzyu of Kyushu University for his kind advice on the preparation of glycol cellulose and also to Dr. M. Sonenberg and Dr. C. Free, Metabolism Laboratory, Sloan-Kettering Institute for Cancer Research, U.S.A., for their help during preparation of the manuscript.
View full abstract
-
XI. Nature of the Interaction between Cytochrome a and Cyanide
YUTAKA ORII, KAZUO OKUNUKI
1964 Volume 55 Issue 1 Pages
37-48
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
1. One molecule of HCN combines with the haematin iron in one molecule of ferri-eytochrome
a. From spectrophotometric ana-lyses the dissociation constant of the complex was 9.2×10
-5M at pH 7.4 and 20°C.
2. Under strictly anaerobic conditions, one molecule of ferrocytochrome
a combines with at least two molecules of HCN, one combining through the haem iron and the other through a formyl group. The latter combination was stable in acidic media but not in alkaline media and the combination was reversed on addition of aldehydes. Cyanhydrin formation was confirmed with porphyrin
a and effects of aldehyde and al-kali were also observed.
3. The absorption spectrum of ferrocyto-chrome
a was markedly altered by aldehyde reagents such as hydroxylamine, hydrazine and nitromethane. The alteration was suggest-ed to be due to formation of an addition compound through a formyl group, which was reactive only in ferrocytochrome
a. 4. From these findings, the nature of the interaction between cytochrome
a and cyanide was schematically illustrated and ar-guments brought forward against the inter-pretation of the phenomena on the basis of the cytochrome
a3 hypothesis. The possibili-ty that the reactivity of the formyl group is dependent on the redox state of haem iron in cytochrome
a was also discussed.
View full abstract
-
I. Physical and Chemical Properties
MAKOTO KAGEYAMA
1964 Volume 55 Issue 1 Pages
49-53
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
A bacteriocin was prepared from the in-duced lysate of
Pseudomonas aeruginosa as a homogeneous, high molecular protein. Elec-trophoretic mobility, sedimentation constant and the amino acid composition were deter-mined. Electron microscopy showed a close similarity of the pyocin to phage tail.
The author expresses his heartily thanks to Dr. Y. Homma, Institute for Infections Deseases, Univer-sity of Tokyo, for the gift of bacterial strains, Dr. S. Kinoshita, Kyowa Hakko Kogyo Co., Tokyo, for the gift of mitomycin C, Dr. Ui and Dr. Tarutani of Gumma University, Maebashi, for the measurement of sedimentation constant, Dr. S. Murakami, College of General Education, University of Tokyo, for electron-microscopy, and Mr. S. Horiuchi of this
department for the amino acid analysis. Thanks are also due to Mrs. K. Ikeda for her held and Professor F. Egami for his guidance and encouragement throu-ghout this work.
View full abstract
-
II. Mode of Production of the Pyocin
KAYOKO IKEDA, MAKOTO KAGEYAMA, FUJIO EGAMI
1964 Volume 55 Issue 1 Pages
54-58
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
Mode of formation of pyocin was studied with S
35-sulfate. From the experiment of differential labeling it was concluded that there was practically no precursor of pyocin in the bacteria before induction. Pyocin was synthesized after a latent of 45 minutes, coincided with the appearance of pyocin activity. There was no synthesis of DNA. The measurement of lacuna formation suggested that the majority of population produced pyocin. The strain R, the pyocinogenic, was found lysogenic too. But the phage had no correlation to the pyocin.
View full abstract
-
III. Biological Properties of the Pyocin
MAKOTO KAGEYAMA, KAYOKO IKEDA, FUJIO EGAMI
1964 Volume 55 Issue 1 Pages
59-64
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
Mode of action of pyocin was studied. Pyocin was readily adsorbed to sensitive bacteria at 0°C, but killing process did not go on at this temperature. Pyocin released ultraviolet absorbing material from sensitive cells.
A muramidase-like enzyme was found in the induced lysate. This enzyme seems to be one of the components of pyocin.
Immunological properties of pyocin were also investigated.
View full abstract
-
MASAYUKI KANDA, HIROSHIGE WATANABE, YOZO NAKATA, TANEAKI HIGASHI, YUKI ...
1964 Volume 55 Issue 1 Pages
65-71
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
1. Gentisic acid was formed from homo-gentisic acid by a rat liver enzyme which was heat stable. The gentisic aldehyde forming enzyme was separated from gentisic aldehyde oxidase during the purification.
2. The gentisic aldehyde forming enzyme and gentisic aldehyde oxidase were purified and the properties of these enzymes were described.
View full abstract
-
YUKIYA SAKAMOTO, TANEAKI HIGASHI, MASAYUKI KANDA, YOZO NAKATA
1964 Volume 55 Issue 1 Pages
72-77
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The enzymatic system catalyzing the formation of gentisic acid from homogentisic acid by the oxidative decarboxylation which had previously been found in liver prepa-rations, was demonstrated to be present in microorganisms.
From a strain of
Pseudomonas aeruginosa two kinds of enzymes, gentisic aldehyde forming enzymes and gentisic aldehyde oxidizing enzyme, were partially purified and their properties were studied.
In the course of enzymatic formation of gentisic acid, gentisic aldehyde was the only detectable intermediate. The enzymatic con-version of homogentisic acid to gentisic aldehyde is probably catalyzed by a single enzyme.
View full abstract
-
MASAYUKI KANDA, HIROSHIGE WATANABE, SETSUO UCHIYAMA, YOZO NAKATA, YUKI ...
1964 Volume 55 Issue 1 Pages
78-80
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
Activity changes of the enzymes involved in the gentisic acid formation in tumor-bearing, fasting and protein-deficient rats were discussed. The activity of the gentisic aldehyde forming enzyme increased and then decreased in tumor-bearing rats. The acti-vity of this enzyme increased in protein-deficient rats and decreased in fasting rats. Gentisic aldehyde oxidase activity decreased in tumor-bearing and fasting rats.
View full abstract
-
III. Characterization of Hydroxy Acids in Depot Fat after Feeding of Ricinoleic Acid
SEIICHI OKUI, MITSURU UCHIYAMA, REIKO SATO, MICHINAO MIZUGAKI
1964 Volume 55 Issue 1 Pages
81-86
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
The hydroxy acids deposited in adipose tissue of rats, which were treated by the successive oral administration of ricinoleic acid or castor oil, were characterized.
Lipids were extracted from adipose tissue of experimental rats followed by the separa-tion of hydroxy acid by column of silicic acid and the analysis by gas-liquid chromatography. In addition to ricinoleic acid, appreciable amounts of 10-hydroxyhexadecenoic, 8-hydro-xytetradecenoic, 6-hydroxydodecenoic and unidentified shorter chain hydroxy acids were detected in depot fat.
The formation of these intermediary hydroxy acids was assumed to be due to the intestinal degradation of ricinoleic acid by microorganisms.
The authors are indebted to Dr. A. Yamaji, Laboratory of Animal Product Technology, Faculty of Agriculture, Tohoku University, for his help in providing the fat emulsions.
View full abstract
-
TAMOTSU TAKETOMI, TAMIO YAMAKAWA
1964 Volume 55 Issue 1 Pages
87-89
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
-
TOSHIO ASAKURA, YOSHIMASA YONEYAMA
1964 Volume 55 Issue 1 Pages
90-91
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS
-
AKIRA KOBATA, KOJI FURUNO, SUZUOKI ZIRÔ
1964 Volume 55 Issue 1 Pages
92-94
Published: January 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL
FREE ACCESS