巻号一覧
45 巻, 2 号
選択された号の論文の8件中1～8を表示しています
- |<
- <
- 1
- >
- >|
-
FUMIO IMAMOTO, KOZO IWASA, KAZUO OKUNUKI1958 年 45 巻 2 号 p. 65-72
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリー1. For the determination of ATP, a simple reaction of hexokinase prepared from yeast was employed by measuring diminution of acid-labile phosphorus. Compared with two other methods, manometric and spectrophotometric, using hexokinase, the present method is easy to use.
3. Illustrative examples are given of analysis of ATP in pure solution and in extracts from physiological materials. The results obtained from these experiments, especially in the latter case, make it quite clear that the acid-labile phosphorus is not the representative of ATP, but phosphorus incorporated into hexose is compatible with the content of ATP.
The expenses of the present work were aided partly by the Scientific Research Grant given to Okunuki from the Ministry of Education.
The authors wish to express many thanks to the Oriental Yeast Ltd. for their kind supply of the pressed yeast.抄録全体を表示PDF形式でダウンロード (498K) -
YASUHARU SEKIZAWA1958 年 45 巻 2 号 p. 73-78
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリーThe metabolite having the molecular formula fitted for C6H10N2O3 obtained from the cultured broth filtrate of Streptonzyces No. 902 was decided as a new metabolite of Streptomyces, ethoxyethene-1, 2-dicarboamide.
Author gratefully thanks to Prof. Dr. Y. Nakamura for his many kind advices, also to Assist. Prof. Dr. S. Tamura for the infrared spectroscopy and Mrs. Y. Baba for the micro elementary analyses. Author was also indebted to Mr. M. Arishima for his advices in microbiological field, and to Mr. M. Ogasawara for pilot plant fermentation and to Mrs. K. Harada for the skilful assistance.抄録全体を表示PDF形式でダウンロード (311K) -
II. UREA DENATURATIONKOZO HAMAGUCHI1958 年 45 巻 2 号 p. 79-88
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリーThe denaturation of lysozyme in solutions of various urea concentrations over a rather wide temperature range was studied by the measurement of viscosity. The results obtained were as follows:
1. The viscosity of lysozyme in 4M urea did not change between 25° and 55° and was the same as that of the native protein.
2. Above 6M urea, the viscosities began to change from about 35° and tended to approach a constant value. This final value was higher with the increase in urea concentration. The viscosity in 10M urea was much greater than that in 8M urea at 25°.
3. The effect of time on the viscosity was scarcely observed. Very small change with time of viscosity was observed in 9 and 10M urea.
4. The effect of pH on the urea denaturation of lysozyme showed that lysozyme was unstable in alkaline medium.
5. In 8M urea containing sodium sulfite the viscosity increased greatly with time. In 6M urea, however, the effect of sulfite was not observed.
6. The results obtained by the present experiments showed the remarkable correspondence with those by the surface chemical method which were reported in the previous papers.
7. Thermodynamic considerations of the denaturation of lysozyme in 8 M urea led to the evaluation of the following thermodynamic parameters: ΔF°=-527 cal./mole, ΔH°=4946 cal./mole, and ΔS°=17.2 ex. at 45°. These values suggest the only minor structural change of lysozyme molecules in 8M urea.
8. The structure of native lysozyme molecule was discussed from the results on the surface-, heat, and urea-denaturation of lysozyme which were so far obtained.
The author expresses his hearty thanks to Prof. T. Isemura for his kind guidance throughout the present work.抄録全体を表示PDF形式でダウンロード (605K) -
MAKOTO NIWA, SHIGETAKA HIGUCHI, FUJIO EGAMI1958 年 45 巻 2 号 p. 89-95
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリー1. 5'-Adenosine monosulphate (AMS) was found to be ineffective as a substrate of 5'-adenylic acid deaminase from rabbit muscle. No inhibition by AMS was observed on the deaminase.
2. Potato 5'-nucleotidase was shown to be inhibited by AMS. Effects of varying pH's on the inhibition were also investigated.
3. Adenosine and ethylene diamine tetraacetic acid are inhibitory to the 5'-nucleotidase.
The authors are indebted to Mr. A. Asano for his generous collaboration in carrying out the determination of ammonia. The expense of this study was defrayed in part by a grant from Seikagaku-Kenkyujo Ltd., to which our thanks are due.抄録全体を表示PDF形式でダウンロード (335K) -
III. EFFECTS OF ENZYME DIGESTED RIBONUCLEIC ACID ON THE HEMOLYSIN FORMATIONKENTARO TANAKA, TAKAYOSHI HAYASHI, SHIZUE MAEKAWA1958 年 45 巻 2 号 p. 97-107
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリー1. Spleen phosphodiesterase digestion of yeast RNA showed no critical change in its potency. The finding by Heppel that the active structure in pancreatic RNase-predigested RNA is resistant to this enzyme was confirmed.
2. Considerable rise in hemolysin-forming potency, such as shown in alkali hydrolysis, was detected during the hydrolysis of yeast RNA by Habuvenom phosphodiesterase. Pancreatic RNase-digested RNA was scarcely affected by this enzyme digestion.
3. Potato phosphodiesterase digestion manifested the effect similar to that of spleen phosphodiesterase digestion on the RNase-predigested RNA. Hydrolysates were separated by means of paper chromatography with isopropanol-water-ammonia system and potency was found only as the starting position.
4. During digestion with RNase of Aspergillus oiyziae, unlike other phosphodiesterase, potency of the yeast RNA and pancreatic RNase-digested RNA diminished very rapidly.
5. Prostatic phosphomonoesterase digestion had no critical erect on the potency of RNA.
6. Some discussions were given as to the possible structure of the active substance.
The authors are indebted to Prof. F. Egami for the interest he has taken and the encouragement he has given during this work.抄録全体を表示PDF形式でダウンロード (2165K) -
IV. FRACTIONATION OF ACTIVE SUBSTANCE FOR STREPTOLYSIN FORMATION AND ITS PROPERTIESKENTARO TANAKA1958 年 45 巻 2 号 p. 109-121
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリーThe active substance for streptolysin formation in pancreatic RNase digests of yeast RNA was fractionated with paper chromatography, dialysis, electrophoresis and ECTEOLA-cellulose column chromatography. The results showed that the active substance is very rich in guanylic acid residue and composed of more than five or six motion ticleotides. Removal of the terminal pyrimidine nucleotide has no remarkable effect on the potency of the active substance.
The author wishes to express appreciation to Prof. F. Egami for his helpful suggestions and encouragement. He is also indebted to Dr. T. Hayashi and Miss S. Maekawa for the determination of potency.抄録全体を表示PDF形式でダウンロード (1850K) -
IV. THE RELATIONSHIP BETWEEN NUCLEIC ACID SYNTHESIS AND AMYLASE FORMATIONMASAYASU NOMURA, JUNKO HOSODA1958 年 45 巻 2 号 p. 123-131
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリーThe relationship between amylase formation and nucleic acid synthesis was studied using 2, 4-dinitrophenol (DNP, 0.5-1.5×10-4M) and 8-aza-guanine (8-AG, 5×10-3M) as inhibitors of nucleic acid metabolism.
Both reagents inhibited the growth of the bacterium and, consequently, the subsequent formation of amylase when added during the logarithmic growth phase. However, DNP showed little inhibitory effect on amylase formation when it was added after the growth ceased, though it could effectively inhibit the incorporation of P32-phosphate and C14-adenylic acid into nucleic acid fraction.
8-AG inhibited amylase formation when added at the stationary phase. This inhibition was reversed by either guanine or yeast RNA. The inhibition was not specific to amylase formation. The general protein metabolism, as measured by the incorporation of S35-methionine into protein, was also inhibited by 8-AG. The inhibition by 8-AG was interpreted not to be due to the inhibition of synthesis of nucleic acid, but due to the formation of abnormal RNA. This interpretation was further supported by the experimental demonstration that DNP effectively eliminated the inhibition by 8-AG.
It was concluded that RNA is necessary for the formation of amylase, but its continuous synthesis (or turnover) from the precursor of nucleoside level may not be required.
The authors wish to express their gratitude to Prof. S. Akabori for his encouragement and helpful suggestion.抄録全体を表示PDF形式でダウンロード (553K) -
III. ENZYMATIC GAS PRODUCTION BY THE REACTION OF NITRITE WITH HYDROXYLAMINEHIDEKAZU IWASAKI, TAKESHI MORI1958 年 45 巻 2 号 p. 133-140
発行日: 1958/02/25
公開日: 2008/11/18
ジャーナル フリー1. When hydroxylamine is added to nitrite in the presence of lactate by using resting cell suspension, both production rate and volume of nitrogen are increased remarkably.
2. Hydroxylamine alone reacts with nitrite and forms a gaseous product, probably nitrous oxide, two nitrogen atoms of which are supposed to originate, one from hydroxylamine and the other from nitrite. This production of gas is inhibited by 10-3M KCN or by a high concentration of hydroxylamine, and the enzyme is destroyed by heating at 100° for 10 minutes. Accordingly there is no other way than to consider that the reaction is enzymatic.
3. Hyponitrite has no effect on production of nitrogen from nitrite; it behaves as an indifferent substance.
4. For NH2OH-NaNO2, system, the Michaelis constants were estimated using cell-free extract. The values are 10-1.2 mole per liter for NH2OH and 10-3.8 mole per liter for NaNO2. Experiments with DMPPD-NaNO2 system indicate that the Michaelis constants are 10-1.5 mole per liter for DMPPD and 10-3.4 mole per liter for NaNO2.
5. It was found that in the DMPPD-NaNO2 system, there is participation by two enzyme components which are separated by a fractionation of the cell-free supernatant obtained by centrifuging at 20, 000×g. using ammonium sulfate.
6. The essential reaction stages in the denitrifying process can be presented in the simple formula
The expences for the work were aided partly by the Grant in Aid for the Scientific Research from the Ministry of Education.抄録全体を表示PDF形式でダウンロード (477K)
- |<
- <
- 1
- >
- >|