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Volume 44, Issue 2
Displaying 1-8 of 8 articles from this issue
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YUJIRO IMANAGA1957 Volume 44 Issue 2 Pages 69-80
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A cell-free extract from Aerobacter cloacae has been found to deaminate GA-6-P and the enzyme is partially purified. In the following reaction,
GA-6-P→F-6-P+NH3
F-6-P has been isolated as Ba salt and identified chromatographically.
2. Crude extract is capable of phosphorylating free GA by the addition of ATP to the system. Kinase activity decreases by dialysis or by ammonium sulfate fractionation.
3. The enzyme preparation shows phosphatase activity towards GA-6-P and G-6-P and is inhibited by NaF (10-2M). Cysteine has no inhibiting effect upon the hydrolysis of GA-6-P.
4. A mechanism of GA catabolism and a new type of enzymic deamination are proposed.
The author takes liberty of expressing his thanks to Prof. S. Akabori of Osaka University and Prof. Y. Matsushima for their kind guidance, and also to Misses Y. Kusanagi, S. Yokoyama, Y. Yamada, T. Oya, K. Maeda, M. Abu, Y. Sekiya, S. Ogura and M. Mikami for their assistance.View full abstractDownload PDF (556K) -
IX. FORMATION OF 7α, 12α-DIHYDROXY-3-KETO-Δ4-CHOLENIC ACID FROM CHOLIC ACID BY A SOIL BACTERIUMTAKEO EGUCHI1957 Volume 44 Issue 2 Pages 81-85
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Some bacterial strains which can utilize cholic acid as the sole source of carbon for growth were isolated from soil.
2. Through the determination of the ultraviolet absorption spectra, it was demonstrated that one of the strains (CE-1) was capable of con-verting cholic acid into intermediates containing 7α-hydroxy-3-keto-Δ4-ene grouping.
3. One of the intermediates which was isolated as its methyl ester from the culture filtrate was probably 7α, l2α-dihydroxy-3-keto-Δ-4-cholenic acid.
In conclusion, the author wishes to express his sincere thanks to Dr. T. Shimizu, Dr. S. Mizuhara, Dr. S. Murakami and Dr. S. Hayakawa for their kind guid-ance throughout this research, and to Mr. M. Seki of Department of Chemistry; Faculty of Science, Nagoya University, for his help in measuring the infrared absorption spectra.View full abstractDownload PDF (262K) -
III. NATURE OF THE ACTIVE FACTOR NECESSARY FOR THE FORMATION OF AMYLASE IN THE LYSOZYME LYSED-CELL PREPARATIONMASAYASU NOMURA1957 Volume 44 Issue 2 Pages 87-97
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe active factor in the boiled cell extract, which stimulates the formation of amylase both by washed cell suspension and in cell-free system, was partially purified.
This substance is a non-dialysable substance, can be precipitated by three volumes of ethanol and also by trichloroacetic or perchloric acid. Deproteinization by chloroform-butyl alcohol does not destroy its activity. Activity is also not destroyed by ribonuclease or protease (trypsin and Bacillus subtilis protease), but largely destroyed by acid hydrolysis (6 N HCl, 100°, 7.5 hours).
From the results of isotopic experiment using S35-labeled cells and S35-labeled factor preparation, it was clearly demonstrated that the active factor is not a precursor of amylase protein, at least with respect to its sulfur, but rather acts as an activator of the processView full abstractDownload PDF (598K) -
HIROO MAENO1957 Volume 44 Issue 2 Pages 99-108
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Among various dehydrogenase activities in the supernatant obtained by bacteriolysis of a halophilic bacterium No. 101, the activities which oxidize glucose, xylose, lactose, maltose, and galactose are halophilic.
2. The glucose dehydrogenase which is characterized by the typical halophilism can catalyze the transfer of hydrogen to dyes of high potentials such as toluylene blue and 2, 6-dichlorophenol indophenol but not to methylene blue, pyocyanine, 2, 3, 5-triphenyltetrazolium chloride and oxygen.
3. The glucose dehydrogenase is rather stable in high salt concentrations but irreversibly loses its activities in the absense of sodium chloride.
4. Not only monovalent cations but also bivalent cations such as Mg++ and Ca++ activate the glucose dehydrogenase. However, Cu++ inhibit completely the activities.
5. Optimum pH varies with the concentration sodium chloride, but Michaelis constant does not.
The author wishes to thank Prof. Fujio Egami for his helpful encouragement and his useful discussions.View full abstractDownload PDF (486K) -
X. A NEW DEGRADATION PRODUCT OF CHOLIC ACID BY STREPTOMYCES GELATICUS 1164SHOHEI HAYAKAWA, YASUO SABURI, IKURO AKAEDA1957 Volume 44 Issue 2 Pages 109-113
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A new degradation product of cholic acid by S. gelaticus 1164 was isolated as its methyl ester from a medium containing sodium cholate and glucose as the carbon sources.
2. The ester was confirmed to be methyl 3α, 7α-dihydroxy-l2-ketobisnorcholanate by its conversion to the known acetyl derivative.
3. 3, 12-Diketo-Δ4, 6-bisnorcholadienic acid, corresponding to a de-hydration product of 7α-hydroxy-3, 12-diketo-Δ4-bisnorcholenic acid which was isolated previously from a medium containing cholic acid as the sole source of carbon, was also isolated as its methyl ester from a medium containing sodium cholate and glucose as the carbon sources.
4. A possible pathway from cholic acid to the formation of 3α, 7α-dihydroxy-12-ketobisnorcholanic acid isolated this time and 3α, 7α-dihydroxy-12-ketocholanic acid previously isolated (1) was discussed.
The authors express their hearty thanks to Prof. T. Shimizu and Prof. S. Mizuhara for their interest and advice in this work, and also to Mr. M. Seki of Department of Chemistry, Faculty of Science, Nagoya University for his help in measuring the infrared absorption spectra.View full abstractDownload PDF (320K) -
MICHIO OGURA, NAOYUKI MIYASHITA, KAZUMI YAMASAKI1957 Volume 44 Issue 2 Pages 115-121
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSΔ4-3-Ketocholenate, 3-ketocholanate and 3-ketoallocholanate were incubated with rat liver homogenate, and the experimental results were as follows:
1. Rat liver contains an enzyme system capable of catalyzing the
reductive process of Δ4-3-ketocholenate. 2. The conjugated double bond system of the 44-3-ketocholenate molecule, which gives a maximum absorption at 250mμ, on incubation was destroyed to some extent.
3. Such a metabolic process was accelerated by TPN, especially in the presence of glucose-6-phosphate, while no acceleration was demon-strated by addition of DPN.
4. On incubation of 3-ketocholanate and 3-ketoallocholanate, it was unable to demonstrate the enzymatic reduction of their C3-ketone group, and on the contrary, they were recovered in increased amounts from the incubation mixture.
The present work was aided by the Grant in Aid for Scientific Research from the Ministry of Education, for which our gratitude is due.View full abstractDownload PDF (373K) -
KAICHIRO KURODA1957 Volume 44 Issue 2 Pages 123-132
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. When human erythrocytes are suspended in the physiological saline solution in the concentration less than 0.1 per cent by volume, filled in a glass vessel and the suspension is made flow by rotation, erythrocytes are orientated so as to take their disk surface parallel to the direction of flow.
2. Therefore, when light perpendicular to that direction is passed through the erythrocyte suspension, the transmitted intensity comes out larger when the suspension is placed in the flowing state than in the resting. Herein exists the cause of the streaming transparency. 3. When the suspension which contains n erythrocytes of optical density i per an unit volume is placed in a vessel of depth r, and the light intensity is Io, the streaming transparency S is expressed theoretically by the following equation:
S=aIo (e-khnir-e-hnir)
where α is a constant, h is the extinction coefficient of the suspension and k means the sphericity of the erythrocyte. The theoretical equation is also confirmed experimentally.
The author wishes to thank heartily Dr. Keizo Kodama, President of Tokushima University, for his kind revision.View full abstractDownload PDF (398K) -
TOKUJI KIMURA, JIRO TOBARI, TAIJI SASAKAWA1957 Volume 44 Issue 2 Pages 133-135
Published: February 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (152K)
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