巻号一覧
59 巻, 6 号
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TAKASHI FUKUMURA1966 年 59 巻 6 号 p. 531-536
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーEnzyme activity for hydrolysis of cyclic and linear oligomers of 6-aminocaproic acid was found in cell extracts of Corynebacterium aacrantiacum B-2(S) and B-2(R), which are strains of bacteria selected by their ability to utilize e-caprolactam.
1. The preparations hydrolyzed cyclic and linear oligomers other than cyclic dimer. The linear analogue and smaller linear oligomers were produced from a cyclic oligomer, and a series of smaller linear oligomers was produced from a linear oligomer. The final product was 6-amino-caproic acid.
2. When strain B-2(R) was cultured on cyclic trimer or tetramer, the cell extract showed a high activity to hydrolyze linear dimer as well as cyclic oligomers. The activity was lower when cells were cultured on ammonium adipate.
3. It seems probable that the cell extract of B-2(R) contains two enzyme systems, one which opens the ring of cyclic oligomers and the other which splits the chain of linear oligomers.
The author wishes to express his thanks to Prof. J. Ashida, Kyoto University, for his kind advice and criticism, and to Dr. K. Kato, Toyo Rayon Co., Ltd., for his valuable suggestions and encouragement in this work.抄録全体を表示PDF形式でダウンロード (1009K) -
TAKASHI FUKUMURA1966 年 59 巻 6 号 p. 537-544
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーTwo kinds of enzymes which hydrolyze oligomers of 6-aminocaproic acid were isolat-ed and partially purified from the cell extract of Corynebacterium aurantiacum B-2(R) by the fractionation with ammonium sulfate followed by DEAE-cellulose column chro-matography.
One of the enzymes cleaves cyclic oligomers and also splits linear oligomers into linear dimer unit. The other enzyme splits linear oligomers into 6-aminocaproic acid unit. The optimum pH of the former was 7.6 for cyclic tetramer and 8.1 for linear tetramer, and that of the latter enzyme was 8.6. Both enzymes did not require any co-factor.
The author wishes to express his hearty thanks to Prof. J. Ashida, Kyoto University, for his kind advice and criticism, and to Dr. K. Kato, Toyo Rayon Co., Ltd., for his valuable suggestions and encoura-gement in this work.抄録全体を表示PDF形式でダウンロード (402K) -
IV. Inactivation by Metal Ions in the Presence of NADH2EIICHI MISAKA, KAZUO NAKANISHI1966 年 59 巻 6 号 p. 545-549
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーThe inhibition of NADH2-lipoamide and NADH2-menadione oxidoreductase activities of enzyme preincubated with NADH2 in the absence of EDTA is found to be due to metal ions contaminating the buffer solution. The activities of the inactivated enzyme are restored by reoxidation of the enzyme in air.
From the inhibitory behaviors of various added metal ions on enzyme activity, these ions could be divided into two groups. Group I ions (Mn++, Fe++ and Co++) strong-ly inhibit the activity of the enzyme when the latter is preincubated with them in the presence of NADH2. But, when the NADH2 in the preincubation mixture is exhausted by a slow reaction of the enzyme with 02, the enzyme activity is restored almost com-pletely to that of the native enzyme. The restoration of the activity of the enzyme after inactivation by Group II metal ions (Zn++, Cd++ and Cu++), however, is very slow and incomplete because of the tight com-bination of these ions with the catalytic dithiol group of the enzyme.
The authors wish to thank Dr. G. Sunagawa, the director of this Laboratory, for his encouragement during the course of this investigation and Dr. M. Nakamura, the superintendent of Sankyo Tanashi Plant, for the supply of a large quantity of the enzyme source.抄録全体を表示PDF形式でダウンロード (395K) -
II. Photochemical Reaction of Adenine and Its PhotoproductsKIHACHIRO UEHARA, TADASHI MIZOGUCHI, SABURO HOSOMI1966 年 59 巻 6 号 p. 550-555
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリー1. The photochemical reaction of adenine in the presence of riboflavin was carried out and its nature was discussed.
2. Hypoxanthine was obtained as a photo-product of this reaction, although yield of the product was extremely low.
3. The rate of degradation of adenine in this reaction was enhanced by the presence of thymine.
The authors wish to thank Matushita Electric Industrial Co., Ltd., for the supply of fluorescent cadmium borate. The authors would like to express their sincere thanks to Dr. G. Chihara for his discus-sions. Their thanks are also due to Miss Y. Aoki, Miss T. Ono and Miss S. Taniguchi for their assis-tances in carrying out the experiments.抄録全体を表示PDF形式でダウンロード (412K) -
III. Photooxidation of CoA and ATPKIHACHIRO UEHARA, TADASHI MIZOGUCHI, YOSHIKO OKADA, JUNJI UMEMOTO1966 年 59 巻 6 号 p. 556-560
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーThe photochemical inactivation of CoA and ATP by visible light in the presence of riboflavin was investigated.
1. The photochemical inactivation of the nucleotides proceeds with the time of irradiation.
2. Oxygen is necessary for the photo-chemical inactivation of CoA.
3. The rate of photochemical inactiva-tion of CoA increases with increasing pH.
4. The photochemical inactivation of the nucleotides in the presence of methylene blueldoes not occur.
The authors wish to express their appreciation to Miss K. Kobayashi for her assistances in carrying out the experiments.抄録全体を表示PDF形式でダウンロード (305K) -
GENJI MATSUDA, KIKUO OGATA1966 年 59 巻 6 号 p. 561-569
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーThe incorporation of C14-L-valine into hemoglobin by intact erythrocytes of the adult chicken, and into total protein by a cell-free system, consisting of microsomcs and L-amino-acid: sRNA ligase fraction, was carried out. The following results were obtained:
1. The incorporating activity of cintat cells from normal erythrocytes is very low as compared with reticulocytes. Puromycin almost completely inhibited this incorporation.
2. The similar magnitude of incorpora-tion was observed in the two main com-ponents of the hemoglobin fraction.
3. Actinomycin D inhibits the incorpora-tion into hemoglobin and the other cellular protein components by intact reticulocytes, especially at the later part of the incubation.
4. The incorporating activity of the cell-free system, consisting of microsomes and the L-amino-acid: sRNA ligase fraction from normal erythrocytes, is very low as compared with that from reticulocytes. The incorporation is dependent on the energy-generating system and is inhibited almost completely by puromycin. Actinomycin D has no effect on the incorporation.
5. Discussion of these results was made on the relationship between RNA biosynthesis and hemoglobin biosynthesis.
The authors thank Dr. H. Sugano, the Department of Chemistry, Faculty of Science, Niigata University, for his cooperation with the ultracentri-fugal study and agar-gel electrophoresis.抄録全体を表示PDF形式でダウンロード (1308K) -
III. Purification and Elemental Analysis of Ceramide Aminoethylphosphonate from Corbicula Complex Lipid MixturesTARO HORI, OSAMU ITASAKA, HIDEO INOUE1966 年 59 巻 6 号 p. 570-573
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーPurification of ceramide aminoethyl-phosphonate from the corbicula, Corbicula
sandai was accomplished by the use of silicic acid column chromatography and by the application of mild alkaline hydrolysis of Dawson. Thus it was found that the pure lipid can be more effectively prepared by the alkaline hydrolysis according to the D a w s o n method than by the silicic acid column chromatography.
In addition, some properties and ana-lytical values of the lipid purified by the alkaline hydrolysis method are presented, and they essentially agreed with those estimated for ceramide aminoethylphos-phonate.
The authors express their cordial thanks to Prof. T. Yamakawa of the University of Tokyo for his kind advice and encouragement.抄録全体を表示PDF形式でダウンロード (919K) -
RYUICHI KATO1966 年 59 巻 6 号 p. 574-583
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーIt was postulated from evidence obtained in the present studies that liver microsomal cytochrome binding carbon monoxide, pro- visionally called P-450, may act as an oxygen-activating component in the oxida-tion of drugs in microsomes.
1. The administration of phenobarbital to rats increased the amount of P-450 in liver microsomes and this found to be increase was almost parallel to that of drug oxidation activity.
2. Starvation caused a slight increase in the amount of P-450, while a sucrose diet caused a decrease. The effect of pheno-barbital in increasing the amount of P-450 was greatly increased in fasting rats. These changes in P-450 were similar to those in oxidation activity.
3. There was little or no P-450 in the liver of the fetus and new-born rats but the amout increased progressively up to 30 days of age and decreased again late. These changes are also similar to the changes in drug oxidation activity.
4. The amount of P-450 was highest in the liver and very low in the kidney and lung. It was negligibly small in the brain, muscle and heart.
Drug oxidation activity also varied in the some way.
5. Administration of phenobarbital and various other compounds increased the amount of P-450 and the degree of this increase was parallel to that of drug oxida-tion activity.
6. In a survey of the distributions of P-450 and drug oxidation activity in different animals the amount of P-450 was found to be highest in the liver of the mouse and lowest in the liver of the cats and drug oxidation activity varied similarly.
6. Drug oxidation activity was inhibited by increase in the concentration of carbon monoxide in the atmosphere and this inhibi-tion was in parallel to the decrease in the amount of free P-450.
Based on these results as well as on the nature of P-450, a possible mechanism for the oxidation of drugs was proposed.抄録全体を表示PDF形式でダウンロード (796K) -
V. Re-examination of Changes in the Optical Rotatory Power of Myosin Caused by Adenosine Triphophate, Inorganic Pyrophosphate and p-Chloro-MercuribenzoateKAZUKO SEKIYA, SANAE MII, KIKUKO TAKEUCHI, YUJI TONOMURA1966 年 59 巻 6 号 p. 584-595
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーThe changes in the -b0 term of optical rotatory dispersion of myosin on addition of ATP, MgPP and PCMB were re-examined under various conditions. The direction and magnitude of the change in the -b0 term (-5 per cent to +5 per cent) on the addition of ATP were dependent on the season of preparation of myosin. The -b0 term decreased mainly with myosin obtained in winter and early spring and increased with myosin obtained in other seasons. The two types of preparation had several properties in common. Thus, the absolute value of the change in -bo caused by ATP was maximal at pH 7.0 to 7.3, increased with decrease in temperature, and was depressed by removal of tightly bound Ca++ from myosin by treatment with PCMB and β-mercapto-ethanol. The change caused by ATP was also observed in NaCl and in the presence of EDTA. A decrease by several per cent in the -b0 term on addition of MgPP was observed with both types of myosin prepara-tion, and was maximal at pH 7.0 to 7.3. An increase in -b0 caused by 4 moles PCMB per 105g. protein and a decrease in -b0 caused by 8 moles PCMB per 105g. protein were observed with both types of myosin.
The spec trophotometric titration curve of tyrosine in myosin, obtained by extrapolat-ing the time-course of the change in optical density at 295 mμ to zero time, only showed an abnormality in the narrow range from pH 9.0 to 10.7, and was unchanged on addi-tion of MgPP. However, the addition of MgPP decreased the amount and the rate of dissociation of those tyrosine residues which dissociate gradually at pH 10.5.抄録全体を表示PDF形式でダウンロード (778K) -
YOSHIAKI KURIYAMA1966 年 59 巻 6 号 p. 596-605
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリー1. Polyglutamyl RNase T1 (PG-T1) and polyalanyl RNase T1 (PA-T1) were prepared by the action of N-carboxyglutamic acid anhydride and N-carboxyalanine anhydride on RNase T1 [EC 2. 7. 7. 26] respectively. Two samples of PA-T1 were enriched with 28.2 and 16.8 alanine residues per enzyme molecule respectively, and the number of polyalanyl chains per enzyme molecule in both of the samples were two, while in the case of PG-T1, three samples were obtained and enriched with 0.6, 2.0 and 2.9 glutamic
acid residues.
2. Chromatographic and paper electro-phoretic properties of RNase Tt derivatives were examined. These RNase Tt derivatives were distinguishable from native RNase T, by chromatography or electrophoresis.
3. PA-T1 was reduced by β-mercapto-ethanol in 8 M urea and inactivated. It was re-oxidized in air and nearly full activity was regenerated.
4. With guanosine 2', 3'-cyclic-phosphate as substrate, the activity and pH-activity curve of PA-T1 and PG-T1 were almost the same as those of RNase T1. At pH 6.0 to 6.7, PA-T1 was significantly more active than RNase T1. The Km values at their optimal pH (pH 7.0) were determined, 2.4×l0-3 M for RNase T1, 2.3×lO-3 M for PA-T1 and 1.3×10-3 M for PG-T1.
5. With RNA as substrate, the pH of optimal activity of PA-T1 was greatly lowered from pH 7.5 for RNase T1 to pH 5.6, while the activities at their respective optimum pH were about the same. The optimum pH of PG-T1 was almost the same as that of RNasc T1.
6. The nucleotide specificity of RNase T1 was not changed at all by its alanylation or glutamylation.
7. The difference spectrum resulting from the interactions of polyalanyl RNase T1 and 2' GMP was observed. The intensity and the pH dependency of absorbancy difference were almost the same as those of RNase T1 and 2'GMP observed by Sat o and Egami (15).
The author would like to thank Prof. F. Egami for his guidance and encouragement. He is also grateful to Dr. J. Koyama, Dr. S. Ishii and Dr. T, Uchida for their valuable advices. And also his appreciation is expressed to Mr. K. Kasai for his guidance in reduction and reoxidation experiment, to Mr. K. Yano for amino acid analysis and to Sankyo Co., Ltd. for supplying “Taka-diastage Sankyo”抄録全体を表示PDF形式でダウンロード (696K) -
TOSHIHARU NAGATSU1966 年 59 巻 6 号 p. 606-612
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリー1. Monoamine oxidase was partially separated from beef brain mitochondria by the combined effects of the use of a detergent Cutscum (1.2%, , pH 7.1) and of sonication (20 kc, 4 minutes, twice). The activity was followed by the disappearance of kynuramine. About 70% of the original activity was liber-ated into solution after the treatments. The activity stayed in the supernatant after the centrifugation at 105, 000×g for 3 hours. The solubilized preparation was unstable. Rapid separation by DEAE cellulose column chro-matography resulted in only 6-fold purifica-tion from the original homogenate.
2. The properties of solubilized brain monoamine oxidase were examined. The enzyme was found to be a sulfhydryl enzyme in so far as it was inhibited by p-chloro-mercuribenzoate. Some metal chelating agents inhibited the activity. The inhibition by sodium diethyldithiocarbamate and euprizone may be indicative of copper in-volvement as a cofactor. The following biogenic amines besides kynuramine could be deaminated by the solubilized enzyme preparation; tryptamine, serotonin, tyramine, dopamine, norepinephrine, and epinephrine. The pH-activity curve showed an optimum between pH 7.5 and 8.0 when kynuramine was used as substrate. Several inhibitors of monoamine oxidase of therapeutic and pharmacological interest, markedly inhibited the activity at concentrations as low as 1×10-5 M.
The author is grateful to Dr. S. Udenfriend (National Institutes of Health, Bethesda) for his encouragement and valuable suggestions. My thanks are also due to Dr. S. Udenfriend and Dr. M. Levitt
(National Institutes of Health, Bethesda) for gifts of monoamine oxidase inhibitors, to Dr. J.W. Daly (National Institutes of Health, Bethesda) and. Dr. D. E. Wolf (Merck Sharp and Dohme Research Laboratories, Rahway) for gifts of kynuramine dihy-drobromide and Cutscum.抄録全体を表示PDF形式でダウンロード (541K) -
NOBU AKAMATSU1966 年 59 巻 6 号 p. 613-618
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーThe nucleotide mixture obtained by alcoholic extraction of Streptomyces griseus was fractionated by Dowex I anion exchange column chromatography and purified by paper chromatography. Uridine diphosphate N-acetyl-D-glucosamine was isolated in an analytically pure state.
The author wishes to thank Prof. T. Arai for his encouragement in this work.抄録全体を表示PDF形式でダウンロード (402K) -
KUNIHIKO SAITO, KIYOMI SATO1966 年 59 巻 6 号 p. 619-621
発行日: 1966/06/25
公開日: 2008/11/18
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YOSHIYA SHINAGAWA, CHIKAKO TANAKA, AKIO TERAOKA, YASUKO SHINAGAWA1966 年 59 巻 6 号 p. 622-624
発行日: 1966/06/25
公開日: 2008/11/18
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AKIRA KOTAKI, MAKOTO NAOI, KUNIO YAGI1966 年 59 巻 6 号 p. 625-628
発行日: 1966/06/25
公開日: 2008/11/18
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TETSUO KATO, NOBUO IZUMIYA1966 年 59 巻 6 号 p. 629-631
発行日: 1966/06/25
公開日: 2008/11/18
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KENTARO TANAKA, HIROSHI TERAOKA, TOMOYUKI NAGIRA, MIKIO TAMAKI1966 年 59 巻 6 号 p. 632-634
発行日: 1966/06/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (176K)
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