All issues
Volume 45, Issue 9
Displaying 1-10 of 10 articles from this issue
- |<
- <
- 1
- >
- >|
-
SIGEHIRO MORITA1958 Volume 45 Issue 9 Pages 651-666
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Aerobic metabolism of acetic acid by an Athiorhodaceae bacterium, Rhodosbseudomonas palustris was investigated under light and dark conditions.
2. By using labeled acetic acid as the substrate, it was revealed that both the methyl- and carboxyl-carbon of the acid were partially evolved as CO2, and partially incorporated in cell material. With the two samples of labeled acetate the relative distribution of C14 in carbon dioxide and cell material was found to be as follows:
_??_ 3. The evolution of C14O2 from carboxyl- or methyl-labeled-both in the light and in the dark-showed some induction period, whereas the incorporation of C14 into cell material occurred without any lag of time.
4. By fractionating the cell material into four portions (water-soluble, lipids, nucleic acids, proteins), the relative rates of C14 incorporation from carboxyl-labeled acetate were investigated, and the results obtained indicated that, both in the light and in the dark, the C14 was first incorporated in the water-soluble fraction, from which it subsequently went partially into CO2 and partially into other fractions, especially rapidly and in a large quantity into the proteinous fraction. The balance between the oxidative (CO2-evolving) and the assimilative metabolism was markedly shifted by illumination in favor of the synthesis of cell material, with a result that the evolution of C14O2 decreased and the translocation of C14 from the water-soluble fraction into other fractions (especially into the proteinous fraction) increased.
It is a pleasure for the author to express his thanks to Prof. H. Tamiya for his continuous guidance and keen intrest throughout this work. His thanks are also due to Prof. A. Takamiy a for helpful advice and kind suggestions. The present work was sup-ported by a grant from the Ministry of Education, which is gratefully acknowledged here.View full abstractDownload PDF (1266K) -
IV. ELECTROPHORETIC COMPOSITION OF EGG YOLK PROTEINSHIROSHI SUGANO1958 Volume 45 Issue 9 Pages 667-674
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. From the results of the electrophoretic studies of the egg yolk and the fractions, the protein composition of the egg yolk has been determined.
2. It has been shown that the lipid and phosphorus contents of the total yolk protein are in good agreement with the values estimated on the basis of the lipid and phosphorus contents of the protein components.
3. The phosphorus distribution in the yolk proteins has been made clear by the similar calculations.View full abstractDownload PDF (476K) -
TAKAYOSHI HIGUCHI1958 Volume 45 Issue 9 Pages 675-685
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (726K) -
I. ENZYMATIC RESOLUTION OF DL-ARGININE INTO ITS OPTICAL ANTIPODESYUKIAKI NADAI1958 Volume 45 Issue 9 Pages 687-692
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A simple procedure for the preparation of acetyl-DL-arginine from benzilidene-L-arginine in a high yield is described.
2. Acetyl-DL-arginine is asymmetrically hydrolyzed by the extract of hog kidney at pH 7.0 or of Takadiastase (commercial) at pH 8.0 to yield L-arginine and acetyl-D-arginine.
3. Satisfactory separation of the above two products of enzymatic hydrolysis is achieved either by the method utilizing insolubilities of acetyl-D-arginine in acidic ethanol and of L-arginine•HCl in methanol or by the method involving precipitation of arginine by flavianic acid.
The author wishes to express his deep gratitude to Prof. Utzino, M. D., for his interest and encouragement throughout the course of the workView full abstractDownload PDF (364K) -
XVI. FORMATION OF 7α-HYDROXY-3, 12-DIOXO-Δ4-CHOLENIC ACID FROM DEHYDROCHOLIC ACID BY CORYNEBACTERIUM SPKEIZO TAMAKI1958 Volume 45 Issue 9 Pages 693-698
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDehydrocholic acid was incubated with Corynebacterium sp. in the synthetic medium containing this bile acid as the sole source of carbon and four transformation products were isolated as crystals. Two out of them were identified 7α-hydroxy-3, 12-dioxo-Δ4-cholenic acid and 3, 12-dioxo-Δ4, 6-chola-dienic acid. However, ultraviolet absorption data of the culture suggests that the latter dienone acid may not be a microbiological transformation product.
The author wishes to express his sincere thanks to Prof. T. Shimizu, Prof. S. Mizuhara and Dr. S. Hayakawa for their kind guidance throughout this research, and to Mr Y. Matsui of Research Laboratory, Shionogi & Co., Ltd. for his help in measuring the infrared absorption spectra and for his valuable criticism.View full abstractDownload PDF (315K) -
ARASUKE NISHI1958 Volume 45 Issue 9 Pages 699-705
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Inactivation of serum trypsin-inhibitor caused by bile and bile acids was investigated. Desoxycholic acid was most effective among various bile acids tested.
2. The inactivation reaction caused by desoxycholate could not be reversed either by dilution or by change in pH.
3. Desoxycholate could not recover the trypsin activity from inhibitor-trypsin complex. Inactivation reaction is, presumably, due to the combina-tion of two molecules of desoxycholate with inhibitor.
Author wish to thank Prof. H. Tamiya and Prof. T. Yanagita for their valuable suggestions and encouragement in this work.View full abstractDownload PDF (373K) -
II. RE-EVALUATION OF ROLE OF ACTION OF CYTOCHROME B2 IN DEHYDROGENATIONS OF LACTATE AND MALATEJINPEI YAMASHITA, TAKEKAZU HORIO, KAZUO OKUNUKI1958 Volume 45 Issue 9 Pages 707-715
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe role of action of the cytochrome b2 contained in baker's yeast lactic dehydrogenase was re-evaluated by using the cytochrome b2 separated from the dehydrogenase as the final electron acceptor.
1. Cytochrome b2 is reduced anaerobically by lactate and by malate in the presence of the yeast lactic dehydrogenase preparation. The reduction by malate is much slow in rate compared with that by lactate as well as in the case where yeast cytochrome c is used as the final electron acceptor.
2. Cytochrome b2 is notably autoxidizable.
3. The reductions of cytochrome b2 by lactate and by malate in the presence of the enzyme preparation are different in optimum pH from those of cytochrome c by both substrates. In the latter cases, the optima pH are at 6.5 and 8.0, while in the former cases, the reductions by lactate and by malate hardly decrease in rate at pH 4.0 and 9.0, respectively.
4. The reduction of cytochrome bg by lactate in the presence of the enzyme preparation is partially inhibited in the presence of FMN or FAD, when it is measured spectrophotometrically.
5. The reduction of cytochrome b2 by lactate in the presence of a test solution of yeast lactic dehydrogenase is almost same in rate as the reduction of cytochrome c in the presence of the test solution diluted forty two times.
Based upon these facts, the role of action of cytochrome b2 in the dehydrogenations of lactate and of malate in the respiring yeast cells was discussed with stress on an importance of a conjugate form between the cytochrome b2 moiety and the dehydrogenase-FMN moiety in yeast lactic dehydrogenase.
We are very grateful to Mr. K. Fujii of Oriental Yeast Co., Ltd., Osaka for supplies of baker's yeast. We should like to thank our colleagues Messrs. M. Nozaki, T. Higashi, H. Matsubara, T. Yamanaka and H. Mizushima for helpful discussions during the course of this work.View full abstractDownload PDF (490K) -
TSUTOMU YASUI, TOSHIYUKI FUKAZAWA, YOSHIO HASHIMOTO, SHOTARO KITAGAWA, ...1958 Volume 45 Issue 9 Pages 717-724
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The deactivation of myosin B-ATPase during storage consisted of two steps: the first pH-independent, a rapid one of the first-order, and the second pH dependent, a slow one. The activity was destroyed partially by the former reaction; complete denaturation occurred only when both of two steps occurred. The first-order rate constants of the first one were 0.70×10-4 and 0.02×10-4. sec.-1 at 30° and 20°, respectively, and the activation energy was about 57 kcal./mole. The second reaction was slow at neutral pH value but was remarkably fast in the alkaline region.
2. The Michaelis constant of ATPase remained almost constant during the denaturation of the protein.
3. The deactivation of myosin proceeded rather similarly with that of myosin B.
4. In the salting-out curve, the peak of the myosin fraction disappeared as the denaturation of myosin B proceeded.
5. When myosin denatured, its ultracentrifugal pattern split into two peaks and the main one spread to some extent.
6. The change of ATP sensitivity during storage coincided completely with that of ATPase under the same condition.
The authors would like to express their cordial thanks to Dr. Y. Tonomura of the Institute for Catalysis for his warm-hearted support and valuable advice during the course of the work and the preparation of the manuscript and also to Mr. T. Nihei of the Low Temperature Institute of this University for his help in kinetic analysis. This study has been aided in part by a grant in aid from the Scientific Fund of the Ministry of Education to the Research Group on the “Protein Chemistry of Meat Products”.View full abstractDownload PDF (432K) -
III. CRYSTALLIZATION OF FISH CYTOCHROME C AND A THIRD METHOD OF PURIFICATIONBUNJI HAGIHARA, KUNIO TAGAWA, ICHIRO MORIKAWA, MASATERU SHIN, KAZUO OK ...1958 Volume 45 Issue 9 Pages 725-735
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA new method, designated as Method III, is described for purification and crystallization of cytochrome c from fish hearts. In this method the starting material is first treated with acetic acid and the cytochrome was extracted at about pH 6 in the absence of added salts. The pigment in the extracts is adsorbed to the resin Amberlite XE-64 equilibrated at pH 6.0 and then eluted after careful washing of the resin with a buffer of pH 7.0. The eluted cytochrome is further treated in similar ways to Methods I and II and crystallized as the reduced form. The yield of crystals is 14μ moles from 1kg. of tunny hearts and 8μ moles from 1kg. of bonito hearts.
The fish cytochrome can also be crystallized by Method II. Method III is, however, superior in causing less modifications. Fish cytochrome c can be crystallized in the oxidized form.
Method III is also very suitable for preparing crystalline cytochrome c from beef heart and pigeon breast muscle.
The authors wish to express their indebtness to Nagase Co., Ltd. for the supply of fish hearts and also to Messrs. T. Okishio and S. Urakabe of Medical School of this University for their assistance.View full abstractDownload PDF (1576K) -
VI. THE MECHANISM OF AMYLASE EXCRETION AND CELLULAR STRUCTURE OF BACILLUS SUBTILISMASAYASU NOMURA, JUNKO HOSODA, HIROSHI YOSHIKAWA1958 Volume 45 Issue 9 Pages 737-744
Published: September 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe trigger mechanism by which the autolytic enzyme of Bacillus subtilis enters into its action was studied. It was found that cyanide or a high concentration of azide, which inhibit respiration of this bacterium, can cause lysis even under aerobic conditions. 2, 4-Dinitrophenol, on the other hand, could not cause lysis, but could stimulate the lysis once the lysis was caused was caused by some trigger mechanism. Chloramphenicol had no effect on anaerobic lysis. Thus, it was concluded that anaerobic lysis may be caused by the activation of a preexisting autolytic enzyme, and this activation may be induced by the reducing condition due to oxygen deficiency.
The relationship between amylase excretion and cellular structure was studied. Lysis due to added cyanide plus 2, 4-dinitrophenol was shown to occur only after the culture began to produce amylase. Protoplasts were also shown to be unstable during this phase.
The participation of the autolytic enzyme in the process of enzyme excretion through the cell wall was proposed and discussed.
Authors wish to express their gratitude to Prof. S. Akabori for his encouragement and helpful advice and to thank to Prof. A. Pardee for reviewing the manuscript.View full abstractDownload PDF (519K)
- |<
- <
- 1
- >
- >|