巻号一覧
49 巻, 3 号
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KATSUHIRA IIDA1961 年 49 巻 3 号 p. 173-176
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーC14-Glucose was incorporated into charo-ninsulfuric acids by mucous gland of Charonia lampas. Amounts of the incorporated glucose were corresponded to 0.2-0.3 per cent of that added into the reaction mixture. The radioactivity of charoninsulfuric acids did not decrease by a dialysis. The glucose incorpora-tion reaction was inhibited by 2, 4-dinitro-phenol. The rate of glucose incorporation into S-poor charoninsulfuric acid was slightly faster than that into S-rich charoninsulfuric acid.
The author wishes to express his gratitude to Prof. F. Egami for his useful advice. This research was supported by grants from the Scientific Research Found of the Ministry of Education and Seikagaku-kenkyusho Ltd. Some of the experiments were carried out in the Marine Biological Station of Nagoya University.抄録全体を表示PDF形式でダウンロード (246K) -
FUMIO IMAMOTO, TADAATSU NUKADA1961 年 49 巻 3 号 p. 177-185
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. Mitochondria particles prepared from guinea pig brain can accumulate noradrenaline by two different mechanisms. While one mechanism involves a nonenzymatic adsorp-tion of the catecholamine to certain anionic sites existing on the mitochondrial particles, the other mechanism represents probably an enzymatic transport of the catecholamine into the inside of the particles. Both mecha-nisms seem to be specific to brain mito-chondrial particles and could not be observed with liver and kidney particles.
2. The transport mechanism is not in-hibited by cyanide, 2, 4-dinitrophenol and fluoride. This fact suggests that the process is not coupled with such energy-generating systems as glycolysis and oxidative phos-phorylation.
3. The transport mechanism appears to be more stable than that responsible for oxidative phosphorylation, but is closely de-pendent on the intactness of particulate structures.
4. The transport is competitively inhibited by cations. It is therefore probable that certain anionic groups of the mitochondrial particles are involved in the transport mechanism.
We wish to thank Prof. R. Imaizumi for his kind advice during this work and the Kao Soap Co. Ltd. for their kind presentation of detergent.抄録全体を表示PDF形式でダウンロード (627K) -
SHO-ICHI SHINODA1961 年 49 巻 3 号 p. 186-190
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (347K) -
I. Purification and Properties of FormokinaseHACHIRO NAKAGAWA, FUJIO SUZUKI, YOSHIRO TAKEDA1961 年 49 巻 3 号 p. 191-199
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. A new formate activating enzyme, formokinase, has been purified approximately 60-fold from extracts of acetone-dried cells of E. coli, strain B, by means of acetone precipi-tation, treatment with calcium phosphate gel, and ammonium sulfate fractionation.
2. Formokinase catalyzes the formation of formohydroxamate in the presence of for-mate, ATP and hydroxylamine. Stoichiomet-ric formation of formohydroxamate, ADP, and inorganic orthophosphate were demonstrated.
3. The reaction requires a sulfhydryl compound (glutathione, cysteine, thioglycolate, or 2-mercaptoethanol) and manganese ion. The participation of folic acid derivatives and CoA in the reaction seems unlikely.
4. Formokinase also catalyzes the forma-tion of ATP from synthetic formyl phosphate and ADP in the presence of manganese ion. Therefore it is concluded that formyl phos-phate is the actual intermediate in the formo-kinase reaction.
5. SH-blocking agents such as p-chloro-mercuribenzoate or heavy metals and EDTA are potent inhibitors of the enzyme.
6. Formokinase is also found in extracts of Pseudomonasfluorescens A3-12, Clostridium welchii and Aerobacter aerogenes.
7. Some evidence differentiating formo-kinase from acetokinase is presented.
The authors wish to express their thanks to Dr. M. Suda for the benefit of many fruitful discussions. The authors also wish to express their gratitude to Dr. R. Y. Stanier, University of California, U. S. A., for a gift of Pseudomonas fluorescens A3-12 and to Dr. M. Yamanaka, Osaka Medical College, for a gift of Clostridium welchii.抄録全体を表示PDF形式でダウンロード (619K) -
V. Chromatographic Resolution of Bovine Globin into the Valylleucyl and Methionyl ChainsSHIGERU SASAKAWA1961 年 49 巻 3 号 p. 200-205
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. Bovine hemoglobin or globin was resolved into two different subunits, valylleu-cyl (α) and methionyl (β) chains, by the acidic urea-treatment followed by the elution chromatography from a column of Amberlite CG-50 of H-phase with the use of urea in 2 N formic acid, increasing the former con-centration stepwise from 4, 6 to 8M.
2. Under the similar conditions, perfor-mic acid-treated globin was also resolved into the both oxidized chains.
The auther is greatly indebted to Mr. Take, Showa College of Pharmacy, for advancing information pertinent to his own experimental data on bovine hemoglobin. Her gratitude is also expressed to Prof. K. Satake for his interest and discussion, and to Mr. Y. Kimura, Miss M. Yoshida and Miss Y. Nagatsuka for their assistance in analysis of the column eluates.抄録全体を表示PDF形式でダウンロード (374K) -
TERUO TAKE1961 年 49 巻 3 号 p. 206-210
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. Bovine hemoglobin or globin was re-solved into two different subunits by paper electrophoresis in 6M urea at pH 6.5.
2. The components moving faster and slower to the cathode, corresponded to valyl-lecyl (α) and methionyl (β) chains, respectively.
3. The both chains seemed to differ from each other not only at their N-terminal posi-tion but throughout the whole structure, from the electrophoretic patterns of their tryptic hydrolysates.
4. The possibility of the asymmetric dis-sociation of hemoglobin (α2β2→α2+β2) under the action of urea, was discussed.
The author is greatly indebted to Mrs. S. Sasakawa, of Prof. Satake's Laboratory, Tokyo Me-tropolitan University, for advance information per-tinent to her own experimental data on bovine hemoglobin. The author's gratitude is also expressed to Prof. K. Satake for his interest and discussion.抄録全体を表示PDF形式でダウンロード (863K) -
XXXV. Formation of Bile Acids from Cholesterol in the Organism of Rana catesbianaTAKAKO MASUI1961 年 49 巻 3 号 p. 211-216
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーAfter injection of cholesterol-4-C14 to nor-mal bull frog, radioactive bile sterols were found in bile as the main metabolites and beside them, radioactive trihydroxycoprostanic acid and cholic acid were identified.
The author wishes to express her deep gratitude to Prof. T. Kazuo for his kind advice throughout this work, and express her thanks to Prof. S. Berg-ström of the Karolinska Institute who has kindly given Hostalene.抄録全体を表示PDF形式でダウンロード (334K) -
YUJI INADA1961 年 49 巻 3 号 p. 217-225
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーThe states of tyrosine residues in insulin, lysozyme and catalase were studied by spec-trophotometric titration based upon the shift with intensification of their tyrosine bands due to the ionization of the phenolic group. On adding alkali to the protein solutions, the transformation of the band occurred in two steps, and instantaneous but partial transformation and a follow-up gradual transformation, from which we could dis-tinguish two types, named ‘free’ and ‘bound’, of tyrosine residues according to their suscep-tibility to ionization caused by alkali. The number of these different types of residues in those proteins as well as their ionization characteristics (pK value, rate constant and the number of hydroxyl ion involved in the ionization) was determined by analysing the ionization curves and by measuring the rates of ionization and their pH dependency. It was revealed from these measurements that, in the case of insulin, three out of four tyro-sine residues were ‘free’ and the remaining one was ‘bound’ possibly by a hydrogen bonding, and that one hydroxyl ion was involved in the ionization of this ‘bound’ residue. In the molecule of lysozyme, one tyrosine residue out of three was found to be strongly hydrogen-bonded, requiring two hydroxyl ions for its ionization. Analysis of catalase molecule showed that out of its total 93 tyrosine residues 26 were in ‘bound’ states, and that of these 19 were ‘strongly bound’ and 7 were ‘weakly bound’. The weakly bound residues seems to be those exposed when the native catalase molecule is split by alkali into its three centrifugally homogeneous subunits. The strongly bound residues were found to require two hydroxyl ions for their ionization, which suggested that they may be hydrogen-bonded in the interior or at the surface of the native cata-lase molecule. The ionization characteristics of various tyrosine residues in the proteins studied were discussed, referring to the data reported by other investigators.
The auther wishes to express his heartfelt thanks to Prof. K. Shibata for his guidance and encourage-ment during this investigation and to Miss. T. Kurozumi for her kind help in the present study. The author also wishes to thank Prof. H. Tamiya very much for many suggestions in the preparation of this manuscript.抄録全体を表示PDF形式でダウンロード (705K) -
VII. Transmaltosidation by Taka-amylase ASHOJI MATSUBARA1961 年 49 巻 3 号 p. 226-231
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. It has been recognized in Taka-amylase A that the enzymatic hydrolysis of aryl-a-maltoside in the presence of various kinds of alcohol is accompanied by the transfer of a part of maltose residue to alcohol, resulting in the formation of corresponding alkyl-α-maltoside.
2. The association of hydrolytic and transfer activities of Taka-amylase A has been considered as suggesting the identity of hy-drolase and transferase, where water and alcohol act respectively as the acceptor of maltose residue.
3. The effect of various factors on the transfer reaction has been studied using methanol as acceptor. The results obtained in respect pH, reaction time and donor and acceptor concentrations seem to show that the same enzyme may both hydrolyse the donor into maltose and phenol compound, and catalyse the transfer of maltose of the donor to an alcohol compound.
The author wishes to express his gratitude to Prof. S. Akabori (Institute for Protein Research, Osaka University) for his helpful advice through this investigation, and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.抄録全体を表示PDF形式でダウンロード (395K) -
VIII. Influence of Substitutents in Phenyl Group on the Enzymatic Hydrolysis of Phenyl-α-Maltoside by Taka-amylase ASHOJI MATSUBARA1961 年 49 巻 3 号 p. 232-239
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. The hydrolyses by taka-amylase A of phenyl-α-maltoside and some of its substitution compounds have been studied; Michaelis con-stants for the dissociation of the enzyme sub-strate complex and the first-order velocity constants for their decomposition have been estimated.
2. First-order velocity constants for the alkaline and acid hydrolyses of most of malto-sides have also been determined.
3. The results have been correlated with the electronic properties of the substituents, as measured by their substituent constants; acid hydrolysis is facilitated by electron-repell-ing substituents but alkaline hydrolysis and the formation and breakdown of the enzyme substrate complex are all facilitated by elect-ron-attracting substituents.
4. The degree of hydrolysis by taka-amy-lase A of the other substituted α-maltosides has been described.
5. A mechanism is suggested for the com-bination and for the decomposition of taka-amylase A with aryl-α-maltosides.
The author wishes to express his gratitude to Prof. S. Akabori (Institute for Protein Research, Osaka University), Dr. Y. Yukawa and Dr. Y. Tsuno (Institute of Scientific and Industrial Research Osaka
University) for their helpful advice through this in-vestigation, and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.抄録全体を表示PDF形式でダウンロード (598K) -
IV. Purification and Properties of a New Type of Alcohol Dehydrogenase, Alcohol-Cytochrome-553 ReductaseTAKEYOSHI NAKAYAMA1961 年 49 巻 3 号 p. 240-251
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. A new type of alcohol-oxidizing en-zyme has been purified from Acetobacter sp.. The resulting preparation had more than one hundred times as high a specific activity as the cell-free extract. The highly purified en-zyme contained a hemeprotein with an absorp-tion spectrum similar to that of cytochrome c, its reduced α-absorption peak being located at 553mμ.
2. In the presence of ethanol, the enzyme reduced various oxidation-reduction dyes in-cluding ferricyanide and 2, 6-dichlorophenol-indophenol, which were either uni- and di-electron acceptors. TPN and DPN were not reduced at all. The hemeprotein was imme-diately reduced by the addition of ethanol.
3. Of the buffers tested, the enzyme was most active in citrate buffer and the optimal pH was 3.8. In this buffer, it was fairly stable from pH 5.0 to 7.0 at temperatures below 45°C. Inactivation of the enzyme proceeded in parallel with the break down of the heme-protein.
4. The enzyme lost 40 per cent of its activity after 24-hours dialysis against deioniz-ed water at 3-4°C. Of the ions tested, only Mg++ activated the dialyzed enzyme slightly, while NH4+, Zn++ Fe+++ and PO4--- were strongly inhibitory.
5. The sulfhydryl reagents tested, includ-ing p-chloromercuribenzoate, did not inhibit the enzyme activity, while all the carbonyl and metal-chelating reagents tested, including semicarbazide and fluoride, were more or less inhibitory.
6. Using ferricyanide as an electron ac-ceptor, the enzyme showed a broad substrate specificity; Almost all the saturated and un-saturated straight chain monoalcohols tested were rapidly oxidized, but iso-alcohols were not. With ferricyanide the Km (moles/liter) was 2.1×10-3 for ethanol, 2.4×10-3 for n-pro-panol, 2.3×l0-3 for n-butanol, 1.2×l0-3 for n-pentanol and 1.3×10-3 for allylalcohol. The Km for ferricyanide was 3.5×10-4 with etha-nol, 2.3×10-4 with n-propanol and 1.6×10-4 with n-butanol.
7. The hemeprotein was rapidly reduced by acetaldehyde in the presence of the co-enzyme-independent aldehyde dehydrogenase (Acetobacter), but not in its absence.
8. Based upon these results, the steric configuration and the active centers of the enzyme molecule were discussed the likelihood that the hemeprotein itself had enzyme acti-vity indicated. It was proposed to name the enzyme “alcohol-cytochrome-553 reductase (Acetobacter)”.
9. The electron-transfer system of the micro-organism was discussed in the light of the results of this series of reports and the fact that acetic acid is accumulated to a great extent as an intermediate product of ethanol oxidation was stressed.
The author would like to express his sincere thanks to Prof. K. Okunuki, Department of Biology, Facul-ty of Science, University of Osaka, Osaka, for his valuable guidance during this study, and to Miss A. Inoue for her technical assistance.抄録全体を表示PDF形式でダウンロード (1535K) -
IX. Fractionation of ClupeineTOSHIO ANDO, FUMIO SAWADA1961 年 49 巻 3 号 p. 252-259
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリー1. Clupeine prepared from Pacific her-ring (Clupea pallasii) was chromatographed on buffered alumina with an eluant of 0.45M aqueous dipotassium hydrogen phosphate, and was fractionated to two main fractions, Y and Z.
2. The fraction Y was further separated to two fractions, Y I and Y II, by counter-current distribution technique using a solvent system consisting of n-butanol, aqueous sodium p-toluenesulfonate and sodium chloride. The fraction Z could not further be fractionated either by chromatography or by countercur-rent distribution.
3. Analyses of N-terminal residues and amino acid compositions of the fractions Y I, Y II and Z were performed. Thus these frac-tions proved to be different from one another in their N-termini and amino acid composi-tions.
4. All the fractions contained arginine, proline, alanine and serine. The fraction Y I contained additional amino acids, threonine, isoleucine, glycine and a small amount of valine. The fraction Y II additionally con-tained valine and threonine as well as traces of isoleucine and glycine. Fraction Z con-tained only valine in addition. The main N-terminus of the fraction Y I was alanine, and that of the fraction Y II was proline. The fraction Z contained only alanine in its N-terminus.
5. The present results on the characteris-tics of clupeine fractions were compared with those obtained in some other laboratories, and some discussions were made on the species specificity of clupeine. This work was aided in part by the Scientific Research Grant from the Ministry of Education.抄録全体を表示PDF形式でダウンロード (518K) -
MASAMI SOEJIMA, KENSUKE SHIMURA1961 年 49 巻 3 号 p. 260-261
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (112K) -
ISAMU SHINO, SHIN-ICHIRO OTSUKA, MASAHIRO TAKAHASHI1961 年 49 巻 3 号 p. 262-263
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (116K) -
SEN-ITIROH HAKOMORI, TAIKO ISHIMODA1961 年 49 巻 3 号 p. 264-265
発行日: 1961/03/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (112K)
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