巻号一覧
48 巻, 4 号
選択された号の論文の17件中1～17を表示しています
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I. CARBOXYMETHYLATION OF HEMOGLOBIN WITH BROMOACETIC ACIDMISAKO NAKATANI1960 年 48 巻 4 号 p. 469-475
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Native, lyophilized and urea denatured hemoglobins were carboxymethylated with bromoacetic acid in the presence of MgO. The optimum pH of the reaction to attack histidine residues in hemoglobin was pH 9, and tyrosine reacted only slightly at this condition. The reaction ended within 10 hours at 30° and about 60 per cent of the total histidines reacted.
2. After treatment with 2 to 8M urea, additional 7 to 22 per cent of the total histidine residues reacted with bromoacetic acid in comparison to those with native one, whereas the lyophilized hemoglobin reacted in the same way as the native.
3. The absorption spectrum at the Soret region was remarkably diminished by the carboxymethylation and particularly a big change was observed with the hemoglobin denatured with 2M urea.
The author wishes to express gratitude to Prof. Y. Oshima and Prof. M. Funatsu for their invaluable advice and criticism during this work, and to Mr. S. Abe for assistance in the preparation of hemoglobin.抄録全体を表示PDF形式でダウンロード (441K) -
II. CARBOXYMETHYLATION OF CATALASE WITH BROMOACETIC ACIDMISAKO NAKATANI1960 年 48 巻 4 号 p. 476-482
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Catalase was treated with bromoacetic acid in the presence of MgO at pH 9. At these conditions, 35 per cent of total diazocoupling groups reacted, and about 20 per cent decrease of the total enzyme activity was resulted.
2. The absorption spectrum changed slightly after the carboxymethylation of the native catalase, whereas 2M urea-denatured catalase showed a remarkable decrease after the carboxymethylation.
3. After treatments of catalase with 2, 6 and 8M urea respectively, additional 11 to 20 per cent of the histidines (10 to 19 moles in one mole of catalase) reacted with bromoacetic acid in comparison with untreated sample. It seems that these urea activated histidine residues are masked in native state, a part of which might be related with secondary structure of the protein.
The author wishes to express her gratitude to Prof. Y. Oshima and Prof. M. Funatsu for their invaluable advice and criticism during the course of this work, and to Mr. S. Abe for his assistance in the preparation of catalase.抄録全体を表示PDF形式でダウンロード (405K) -
II. THE SPECIFICITY OF INSULIN NEUTRALIZING ANTIBODY AND EXPERIMENTAL DIABETESMASAYASU KITAGAWA, KAORU ONOUE, YUTAKA OKAMURA, MOTOAKI ANAI, YUICHI Y ...1960 年 48 巻 4 号 p. 483-489
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Guinea pig immune serum against ox insulin neutralized ox, pig, whale, dog, rabbit and bonite insulin but not guinea pig insulin.
2. Neutralization occurred also for mouse and rabbit endogenous insulin. Diabetic syndrome due to insulin deficiency was induced in mice by injections of guinea pig immune serum.
3. Immunized guinea pigs showed skin reaction for insulin from ox, pig and whale.抄録全体を表示PDF形式でダウンロード (395K) -
IX. SILICIC ACID CHROMATOGRAPHY OF MAMMALIAN STROMA GLYCOLIPIDSTAMIO YAMAKAWA, REIKO IRIE, MICHIKO IWANAGA1960 年 48 巻 4 号 p. 490-507
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Silicic acid column chromatography was applied to the purification of crude glycolipids obtained from human, equine, bovine, sheep, cat, guinea-pig blood cells stroma as well as rabbit erythrocytes.
2. Glycolipids were separated to methanol-ether soluble and chloroformmethanol soluble materials and each of these was further divided by chroma-into ceramide-oligohexoside and mucolipid.
3. Chromatographic pattern and nature of mucolipids were remarkably peculiar to each animal secies. Generally speaking, muco lipids of human, sheep, guinea-pig and rabbit contain hexosamines, whereas those of equine and cat sialic acids instead.
4. Blood group active lipid as well as Forssman hapten were purified by this procedure from human, sheep and cat erythrocytes.
5. Infra-red spectra of these and other glycolipids are presented.
The authors wish to express their gratitude to Dr. T. Takeuchi and Dr. M. Kuniyuki for the supply of blood. They also thank Dr. Y. Ichikawa and Mr. J. Ozaki for blood group assay, to Mr. S. Yamamoto for performance of ultracentri-fugation and finally to Mr. C. Sato and Miss. Y. N atsume for technical assistance.
The expence of the work was aided by the Scientific Fund, furnished by the Ministry of Education, for which the authors also wish to thank.抄録全体を表示PDF形式でダウンロード (1620K) -
II. PURIFICATION AND PROPERTIES OF SULFATASESNORIKO TAKAHASHI1960 年 48 巻 4 号 p. 508-514
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Sulfatases (arylsulfatase, glucosulfatase and cellulose polysulfatase) in the liver extract of Charonia lampas have been separated from coexisting polysaccharases by selective precipitation of polysaccharases with trypaflavin and subsequently by selective adsorption of sulfatases on CM-cellulose, DEAE-cellulose, or by electrophoresis.
Arylsulfatase, glucosulfatase and cellulosepolysulfatase were purified about 20-fold, 160-fold and 6-fold respectively, of the crude extract.
2. The properties of sulfatases were studied with the purified enzyme preparation. pH optimum of glucosulfatase and cellulosepolysulfatase were 5.8 and 6.2 respectively. Arylsulfatase, glucosulfatase and cellulosepolysul-fatase were most stable at pH 5-6.5, pH 5.0 and pH 7.0 respectively at 4°.
The author thanks Prof. F. Egami for his interest and encouragement. A part of the expense of this study was defrayed by a grant from the Ministry of Education and from, Seikagaku-Kenkyusho Ltd., to which her thanks are due. Some of the experiments were carried out in the Marine Biologoical Station of Nagoya University.抄録全体を表示PDF形式でダウンロード (349K) -
I. EFFECTS OF EGG YOLK LECITHIN ON THE REAGENT OF CEPHALIN-CHOLESTEROL-FLOCCULATION TESTMASAHARU KUROKAWA, KYOKO HOTTA, TOMOKO YOSHIMURA, SAKUO TOMOE, ICHIRO ...1960 年 48 巻 4 号 p. 515-524
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Phosphatidyl serine fraction prepared by Folch's method from crude cephalin was the most reactive factor in CCF reaction, as compared with other fractions.
2. Lecithin inhibited the precipitation of serum proteins or λ-globulin by phosphatidyl serine suspension. The CCF reagent with constant potency could be prepared by mixing of lecithin with phosphatidyl serine fraction in a proper ratio.
3. Lecithin also stabilized the CCF reagent suspension for a few days' storage.抄録全体を表示PDF形式でダウンロード (534K) -
III. SUBSTRATE-SPECIFICITY OF BAKER'S YEAST LACTIC DEHYDROGENASEJINPEI YAMASHITA1960 年 48 巻 4 号 p. 525-538
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Baker's yeast lactic dehydrogenase can utilize ferricytochrome c and phenazine methosulfate as electron acceptors in the oxidation of lactate and α-hydroxybutyrate.
2. Lactate is oxidized twice as rapidly as α-hydroxybutyrate. In the reduction of ferricytochrome c, optimum pH's are at 6.0 for lactate and 5.5 for α-hydroxybutyrate. With phenazine methosulfate, optima are at pH 7.3 and 6.8, respectively.
3. There is no summation of activity in the presence of both lactate and α-hydroxybutyrate during reduction of ferricytochrome c or oxygen uptake with phenazine methosulfate.
4. KM values for lactate and α-hydroxybutyrate are 6.4×10-4M and 1.6×10-3M, respectively, at pH 6.0, and 20°.
5. Heat treatment decreases the activity towards both substrates in parallel.
Results suggest that baker's yeast lactic dehydrogenase catalyzed the oxidation of both lactate and α-hydroxybutyrate.
The author would like to express his thanks to Prof. K. Okunuki, Dr. T. Horio and all his colleagues in this laboratory for their valuable guidance and helpful discussion through this work, and to Dr. T. P. Singer, Edsel B. Ford Institute for Medical Research, Detroit, for a gift of phenazine and to Mr. K. Fujii in Oriental Yeast Co., Ltd. Osaka, for supplies of baker's yeast.抄録全体を表示PDF形式でダウンロード (729K) -
TARO OKAZAKI, SUMIKO TAGUCHI, KEIZO TSUSHIMA1960 年 48 巻 4 号 p. 539-547
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. The thermodynamic constants for the reactions of metmyoglobin with sodium azide and potassium thiocyanate were determined as follows:
a) for the reaction with azide. (pH 7.0, at 20°) ΔH=-16.45 Kcal/mole, ΔF=-6.10 Kcal/mole, ΔS=-35.3 cal/mole/deg.
b) for the reaction with thiocyanate. (pH 7.0, at 20°) ΔH=-10.56 Kcal/mole, ΔF=-3.31 Kcal/mole ΔS=-24.7cal/mole/deg.
ΔS values for both reactions did not differ significantly from the values which had been determined by other workers for various reactions of hemoglobin and myoglobin.
2. The dissociation constants for the heme linked acid groups of metmyoglobin, azide-metmyoglobin and thiocyanate-metmyoglobin were calculated to be 10-6.11, 10-6.63 and 10-6.56 at 20°, respectively. The heats of dissociation of these groups were calculated to be about 6 Kcal/mole in every case, indicating that the heme linked acid group of myoglobin might be the imidazole group of a histidine.
3. Some speculations were made on the mechanism of the Bohreffect.
The authors wish to express their gratitude to Prof. K. Kaziro for his advices and useful discussions during the course of this work.
The present work was supported by the Science Research Fund of the Ministry of Education. The essential part of this study was published in Japanese (15).抄録全体を表示PDF形式でダウンロード (485K) -
II. THE EFFECT OF SULFITE ON THE METABOLISM OF SULFATE AND ITS CONVERSION INTO ORGANIC FORM IN EXCISED LEAVESTADASHI ASAHI, TAKAO MINAMIKAWA1960 年 48 巻 4 号 p. 548-556
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーIt has been observed that the simultaneous infiltration of S35-labeled sulfate and non-labeled sulfite into the excised mung bean leaves, which were able to convert sulfate-sulfur into organic form, resulted in inhibition of the formation of S35-labeled organic compounds. This inhibitery effect of sulfite on the metabolism of sulfate sulfur may be explained on the basis of the preferential utilization of sulfite as a source of sulfur for the synthesis of sulfur-containing organic compounds. It was also observed that sulfate-S35 was converted to sulfite-S35. Futhermore, sulfite-S35 was readily converted to sulfur-containing amino acids such as cystine, methionine, cysteine-sulfinic acid, and some unidentified substances. These results support the hypothesis that sulfite is an intermediate in the biosynthetic pathway of sulfur-containing amino acids from sulfate.
The authors are indebted to Prof. I. Uritaniin Laboratory of Biochemistry for his kind discussions during this investigation, and thanks are also due to Miss N. Harada in Laboratory of Food and Nutritional Chemistry of this Department for her partial participation in this work.
Some of the data were presented at the Annual Meeting of the Agricultural Chemical Society of Japan, Tokyo, April, 1958.抄録全体を表示PDF形式でダウンロード (521K) -
TERUHIKO BEPPU, KEI ARIMA1960 年 48 巻 4 号 p. 557-568
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーI. A strain of Achromobacter having a capacity for decomposing Ls-alloisocitrate, which had been believed to be an unnatural diastereoisomer of isocitric acid, was isolated.
2. From this organism an adaptive enzyme, DPN-specific L-alloisocitric dehydrogenase, which oxidizes the acid to α-ketoglutaric acid, was extracted. The reaction was found to be irreversible and seemed to require no metals nor other cofacters.
3. A constitutive enzyme, DPN-specific α-hydroxyglutaric dehydrogenase was for the first time found in this bacterium. Dependence of the enzyme on Mg++ or Mn++ was revealed only after the dialysis against EDTA.
4. Anaerobic dismutation of L-alloisocitric acid to α-hydroxyglutaric acid was proved in a crude cell-free extract of the organism.
5. The activity of oxidizing α-hydroxyglutaric acid was found to be widely distributed among different species of bacteria. It was discussed that the α-hydroxyglutaric dehydrogenase may take a role of DPNH-acceptor system in vivo.
6. A procedure was devised to estimate L-alloisocitric acid manometrically using the crude extract of the bacterium with EDTA and semicarbazide.
The authors wish to express their gratitude to Dr. K. Sakaguchi, The Institute of Physical and Chemical Research, Tokyo, for his kind advice throughout this work. Their thanks are also due to Dr. K. Komagata, The Institute of Applied Microbiology, University of Tokyo, for his valuable advice in the taxonomical studies of the organism.抄録全体を表示PDF形式でダウンロード (735K) -
VI. EFFECT OF ALDEHYDE REAGENTS ON CYTOCHROME ASHIGEKI TAKEMORI, ICHIRO SEKUZU, KAZUO OKUNUKI1960 年 48 巻 4 号 p. 569-578
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Cytochrome oxidase activity is strongly inhibited by aldehyde reagents such as hydazine, phenylhydrazine, hydroxylamine and sodium bisulfite at a concentration of 10-3M. The inhibition occurred rapidly and was readily reversed by dialysis.
2. Analysis of the nature of the inhibition suggests that there are both competitive and non-competitive inhibitors with cytochrome c.
3. The absorption spectrum of reduced cytochrome a changes towards shorter wavelengths in the presence of hydroxylamine, while there is no marked shift in the position of the peaks on addition of the other aldehyde reagents.
4. Hemin a and porphyrin a shift their absorption bands towards shorter wavelengths on addition of aldehyde reagents. These shifts in the absorption bands are attributable to the formation of an oxime or a hydrazone with the formyl group.
5. The role of the formyl group of cytochrome a in the cytochrome oxidase reaction is discussed on the basis of these findings.
The authors thank Messrs. Y. Orii and K. Ohnishi for their help and discussion during this investigation.抄録全体を表示PDF形式でダウンロード (598K) -
II. AN IMPROVED METHOD FOR THE PREPARATION OF DIPHOSPHOPYRIDINE NUCLEOTIDE FROM BAKER'S YEAST USING ION EXCHANGE RESINSMASATERU SHIN, YUKIHIKO HAMURO, KAZUO OKUNUKI1960 年 48 巻 4 号 p. 579-583
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーHighly purified DPN was prepared in good yield by a simple method, in which the main procedures were carried out by ion exchange resins. About 500 to 600mg. of DPN was obtained from 2kg. of fresh Baker's yeast by this method with 85 to 90 per cent purity.
The adsorption of DPN by two types of cation exchange resins, the polyphenol resin, Duolite C-10, and the polystylene resin, Duolite C-25 was compared under different conditions.
The authors wish to express their thanks to Dr. B. Hagiliara, Dr. K. Tagawa and Dr. I. Sekuzu for their kind advice and helpful discussion during the present investigations and also to the Oriental Yeast Co. Ltd. for a gift of Baker's yeast.抄録全体を表示PDF形式でダウンロード (302K) -
IV. PARTICIPATION OF PYRIDOXAL PHOSPHATE IN THE ACTIVE TRANSFER OF L-AMINO ACIDS THROUGH THE INTESTINAL WALLKEISHI UEDA, HITOSHI AKEDO, MASAMI SUDA1960 年 48 巻 4 号 p. 584-592
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリー1. Using everted rat intestines in vitro, it was found that the rate of transfer of L-histidine from the mucosa to the serosa was suppressed by DNP and the original rate was restored only by pyridoxal phosphate.
2. Using the perfusion technique in vivo, evidence was found that L-and not D-penicillamine inhibited L-methionine absorption.
3. A study was made of the effect of L- and D-penicillamine on pyridoxal phosphate-requiring enzymes such as tryptophanase and transaminase. Only the L-isomer inhibited enzyme activity strongly, though both isomers could combine with pyridoxal phosphate. After thiazolidine formation, both L- and D-penicillamine strongly inhibited these enzymes.
4. From these results, the hypothesis is proposed that there may be a carrier protein involved in amino acid absorption from the intestine which is associated with pyridoxal phosphate.抄録全体を表示PDF形式でダウンロード (505K) -
VI. HYDROLYSIS OF PROTEIN BY STREPOMYCES GRISEUS PROTEASEMASAO NOMOTO, YOSHIKO NARAHASHI, MITSURU MURAKAMI1960 年 48 巻 4 号 p. 593-602
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーSubstrate specificity of Streptomyces griseus protease has been ivestigated by the following three methods; 1) Analysis of hydrolysing course of protein, 2) Assay for extent of hydrolysis of protein, 3) Quantitative analysis of amino acids liberated from protein.
It was found that the protease had an extremely broad substrate specificity and was capable of hydrolysing almost all peptide-bonds in proteins, until the majority of amino acids constructing the protein were liberated as the respective free amino acids. Therefore, the extent of hydrolysis of proteins was estimated to reach upward of 70-90 per cent in contrast to acid hydrolysis. So far as is known in the literature, there is nothing as strong as the present protease. It is felt that the protease will help to develop many new industrial and scientific techniques.
A suitable method for preparing amino acid mixtures by this protease is described in this paper, together with some other applications of this protease.
The authors wish to express their thanks to Dr. T. Akahira Dr. M. Yanagita, Prof. K. Sakaguchi, Prof. S. Akabori and Prof. K. Okunuki for their kind guidance and useful suggestions. The authors are also grateful to Mr. S. Fujita for preparation of enzyme, to Mr. J. Kirimura for bio-assay of amino acids and to Mr. M. Yamasaki for measurement of amino-nitrogen by van Slyke volumetric method.
The present work was aided in part by a grant of the Scientific Research Fund of the Ministry of Education for which the authors wish to thank the Ministry.抄録全体を表示PDF形式でダウンロード (617K) -
I. PURIFICATION AND PROPERTIES OF TAKA-ACYLASE FROM TAKA-DIASTASEMASAYORI INOUYE, SHIRO AKABORI1960 年 48 巻 4 号 p. 603-616
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーTaka-acylase was purified ca. 1000 fold from taka-diastase by starch column-zone electrophoresis.
The enzyme is activated only by Co++ and various other metal ions are inhibitory. It was found that both Co++ and metal ions having an inhibitory action protected the enzyme from heat denaturation when they were present together with sodium acetate or sulfate.
A pH optimum was found at 8.6 at low concentrations of Co++. At higher concentrations of Co++ two pH optima were observed at 8.0 and 10.0.
Substrate specificity of Taka-acylase was compared with that of pancreas carboxypeptidase.
Some other properties of the enzyme were investigated and discussed.
The authors wish to express their gratitude to Dr. A. Tsugita for his valuable advice throughout this investigation and also to Sankyo Co., Ltd. for kindly supplying “Taka-diastase Sankyo”.抄録全体を表示PDF形式でダウンロード (716K) -
KUNIO YAGI, TOSHIHARU NAGATSU, IKUKO NAGATSU ISHIBASHI1960 年 48 巻 4 号 p. 617-620
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーThe dynamic changes of the fluorescence spectrum and of the absorption spectrum during the condensation reaction of DOPA and ethylenediamine were measured. The results indicate that the reaction proceeds in at least two steps and that more than 90 minutes of reaction at 50° is required to obtain a constant fluorescent product.抄録全体を表示PDF形式でダウンロード (177K) -
KUNIO YAGI, JUN OKUDA, A. A. DMITROVSKJI1960 年 48 巻 4 号 p. 621-622
発行日: 1960/10/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (122K)
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