巻号一覧
52 巻, 1 号
選択された号の論文の12件中1～12を表示しています
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XLV. The Metabolism of 3α, 7α, 12α-Trihydroxy-coprostane in Toad Liver HomogenateSHOICHI ENOMOTO1962 年 52 巻 1 号 p. 1-4
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリーIt was demonstrated that the toad liver homogenate oxidizes 3α, 7α, 12α-trihydroxy-coprostane to 3α, 7α, 12α, 26-tetrahydroxy-25-Dcaprostane and 3α, 7α, 12α-trihydroxy-25-Dcoprostanic acid.抄録全体を表示PDF形式でダウンロード (229K) -
HIROMICHI HASEGAWA1962 年 52 巻 1 号 p. 5-11
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. Lactate dehydrogenase was prepared from fresh baker's yeast according to the method of Bach et al. (9).
2. The oxidation-reduction potential of cytochrome b2 was measured at various pH of the medium and at 25°C. The value obtained was +0.122 volt in the pH range from 6 to 8. At pH-values higher than 8.0, the E'0-value decreased with the decreasing concentration of hydrogen ion.
3. The absorption spectrum of flavin mononucleotide attached to the enzyme could be measured by titrating the reduced enzyme with methylene blue solution under anaerobic conditions. The oxidized form of the flavin moiety showed absorption maxima at 385 and 445mμ.
4. The enzyme activity was inhibited by riboflavin which was found to replace the flavin mononucleotide attached to the enzyme protein.
The author wishes to express his gratitude to Profs. H. Tamiya and Y. Ogura for their guidance in this work. Thanks are also due to the Oriental Yeast Co. for the supply of baker's yeast.抄録全体を表示PDF形式でダウンロード (502K) -
HIROMICHI HASEGAWA1962 年 52 巻 1 号 p. 12-15
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. The L(+)-lactate dehydrogenase isolated from yeast cells was found to be quite innert against D(-)-lactate. Its activity towards L(+)-lactate is inhibited by higher concentrations of the substrate, and this phenomenon may be explained by the formation of an inactive complex (ESS) resulting from the reaction between the Michaelis complex (ES) and the substrate.
2. The pH-dependency of the enzyme activity was investigated using methylene blue as hydrogen acceptor. The optimum pH was found to be in the range of 7.2 to 7.6.
3. The course of denaturation of the enzyme molecule was followed at 0°, 15°, 25° and 33°C. The denaturation at each temperature was found to proceed according to the first order kinetics with respect to the enzyme concentration. The activation energy of denaturation process was calculated to be 7.15 Kcal. per mole.
The author wishes to express his gratitude to Profs. H. Tamiya and Y. Ogura for their guidance in this work. Thanks are also due to the Oriental Yeast Co. for the supply of baker's yeast.抄録全体を表示PDF形式でダウンロード (264K) -
I. Acid-denaturation and Its Reversal by NeutralizationTOSHIO TAKAGI, HIROKO TODA1962 年 52 巻 1 号 p. 16-27
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. Acid-denaturation of Taka-amylase A in the vicinity of pH 2 and its renaturation by neutralization were followed by measuring enzymatic activity and optical rotation.
2. Acid-denatured Taka-amylase A and renatured Taka-amylase A were examined by measuring enzymatic activity, chromatographic behavior, optical rotation, viscosity, titration curve, and sedimentation behavior.
3. It was found that most of acid-denatured Taka-amylase A molecules were restored to the original structure by neutralization in favorable conditions. Crystalline Taka-amylase A was obtained from neutralized Takaamylase A solution. The optimum pH range for renaturation was pH 6 to 9.5. Renaturation was inhibited markedly by the increase in ionic strength.
4. The destruction of Taka-amylase A molecule by acid is limited as compared with that by 8M urea, and the partially denatured molecule is very stable in the vicinity of pH 2. It appears that most of helical structure is retained in acid-denatured Taka-arnylase A.
5. Taka-amylase A is more unstable in the vicinity of pH 3 than below pH 2. This fact might be due to proteolysis by acid Takaprotease (optimum pH=3) contained as impurities.
The authors wish to express their gratitude to Prof. T. Isemura for his kind guidance and to Prof. S. Akabori for his encouragement. They also wish to thank Dr. K. Hamaguchi for the discussion of the problem, and Sankyo Co., Ltd. for a supply of “Takadiastase Sankyo”. Part of this work was done during tenure of the post doctoral fellowships of the Japanese Society for the Promotion of Science.抄録全体を表示PDF形式でダウンロード (1729K) -
VIII. Reaction of Cytochrome a with Chemically Modified Cytochrome c and Basic ProteinsSHIGEKI TAKEMORI, KEISHIRO WADA, KAZUKO ANDO, MAMORU HOSOKAWA, ICHIRO ...1962 年 52 巻 1 号 p. 28-37
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. Cytochrome c, which contains more than 32 per cent of the amino groups in the acetylated form or more than 22 per cent in the succinylated form showed no activity in the cytochrome oxidase reaction. The ability of the modified cytochrome c preparation to reduce cytochrome a decreased with the degree of modification.
2. The activity of TCA-modified cytochrome c decreased more rapidly than the ability to reduce cytochrome a. 3.
The binding of TNBS with 3.6 moles of the ε-amino groups of the lysine residues per mole of cytochrome c caused almost complete loss of the cytochrome oxidase activity.
4. The cytochrome oxidase activity of guanidinated cytochrome c preparations was as high as that of native cytochrome c.
5. Protamines and poly-lysine showed a great inhibition on cytochrome oxidase activity. However, copolymer containing glutamic acid and lysine showed little inhibitory effect.
6. The reaction mechanism between cytochromes a and c is discussed on the basis of the above results.
We wish to express our thanks to Prof. Noguchi, J., University of Kanazawa, Prof. Satake, K., Tokyo Metropolitan University, Dr. Iwai, K., University of Tokyo and Dr. Hamaguchi, K., the Institute of Protein Research, University of Osaka for their generosity in providing samples of compounds used in this study. We would also like to thank Messers. Orii, Y., and Ohnishi, K., in our Laboratory for helpful discussion during the course of this work.抄録全体を表示PDF形式でダウンロード (753K) -
YOSHIHIKO FUJITA, AKIHIKO HATTORI1962 年 52 巻 1 号 p. 38-42
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. Changes occurring during the formation of phycoerythrin in the cells of a bluegreen alga Tolypothrix tenuis under various experimental conditions were investigated, with special reference to the levels of nitrogenous compounds, carbohydrates and keto acids.
2. During the period of pre-illumination of algal cells with fluorescent light in CO2-containing air and in the absence of N-source, a marked increase in contents of polysaccharides and keto acids was observed, while no significant change was noticed in amounts of nitrogenous compounds (amino acids, amides and protein) and soluble carbohydrates.
3. On subsequent incubation under darkaerobic conditions, and in the presence of added N-sources (nitrate or ammonia), a temporary increase in contents of amino acids and amides occurred, immediately followed by the rise in levels of protein and phycobilin chromoproteid (phycoerythrin in the present case).
4. A marked decrease in methanol-insoluble carbohydrates (probably cyanophycean starch) was found to occur in pace with the assimilation of the added nitrogen source, indicating the role of this class of substances as sources of energy and carbon in the assimilation of nitrogen. The levels of keto acids (pyruvic and a-ketoglutaric) were also found to decrease at the same phase of assimilatory process, a change indicating the participation of these substances in the formation of amino acids.
5. The experimental results obtained were discussed with reference to the synthesis of phycobilin chromoproteids.
The authors express their gratitude to Prof. H. Tamiya and Prof. A. Takamiya for their encouragement and criticism throughout this work. Thanks are also due to Profs. A. Watanabe and S. Hattori for their interest. This work was supported by, grants from the Ministry of Education and the Waksman Foundation of Japan.抄録全体を表示PDF形式でダウンロード (412K) -
Studies on the Metabolism of Rat-Ascites-Tumor with Nitrogen Mustard Sensitive and Resistant StrainsVII. Effect of Ubiquinone and Vitamin K3 on Succinate- and α-Glycerophosphate-Neotetrazolium ReductaseYOSHIAKI MIURA, YOSHIRO ASO, YOSHIYA MASHIMA, ICHIRO NAGATA1962 年 52 巻 1 号 p. 43-49
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. The activation of succinate- and α-glycerophosphate-NT reductase in the mitochondria of rat ascites hepatoma were compared with those in the mitochondria of normal and regenerating liver.
2. Ubiquinone (45), (50) isoprenologue, and vitamin K3 showed remarkable stimulation on NT reductases. Ubiquinone (0) has rather an inhibitory effect for the enzyme system.
3. The mitochondrial a-glycerophosphate-NT reductase was characteristic for the hepatoma. No formazan production was observed by hepatic mitochondrial preparation when α-glycerophosphate was used as substrate.
4. The NT reductase activities of all mito-chondrial preparations were largely sensitive to the addition of antimycin, PCMB, and with lesser extents to barbiturates and uncouplers.
5. In the presence of vitamin C, the same level of NT reductase activity was obtained in AH strain regardless of the kind of substrates.抄録全体を表示PDF形式でダウンロード (514K) -
II. Hemagglutinin Separated from Crystalline Ricin and Its Molecular WeightTAKAO TAKAHASHI, GUNKI FUNATSU, MASARU FUNATSU1962 年 52 巻 1 号 p. 50-53
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリーA component containing mainly hemagglutinin separated from crystalline ricin by hydroxyl apatite was purified by DEAE-cellulose and subsequently CM-cellulose column chromatography. The hemagglutinin thus obtained was found to be homogeneous by examination with moving boundary electrophoresis and sedimentation in the ultracentrifuge. In addition, this component was able to agglutinate 0.2ml. of a 4% suspension of washed rabbit erythrocytes with 0.001μg. N. Its sedimentation constant (s20) was found to be 6.39×l0-13. The molecular weight measured by the light-scattering method was 98.000.
We wish to express our thanks to Dr. Martin Sonenberg, Head, Metabolism Laboratory, Sloan-Kettering Institute for Cancer Research, for his help during preparation of the manuscript.抄録全体を表示PDF形式でダウンロード (1545K) -
IV. A Particulate Fraction Controlling the Specificity of Fibroin Synthesized in a Cell-free SystemIWAO SUZUKA, SHIGEAKI TANAKA, KENSUKE SHIMURA1962 年 52 巻 1 号 p. 54-58
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリー1. The comparative studies on the incorporation of C14-glycine, C14-alanine and C14-leucine into proteins were carried out by using the various combinations of the cellular fractions prepared from Bombyx mori silkgland, Attacus ricini silkgland and rat liver.
2. The relative amounts of the C14-amino acids incorporated into protein resembled the amino acids composition of the proteins which are preferentially synthesized in the particulate fraction, regardless of the source of the supernatant enzyme combined.
3. It was suggested that the specificity of nascent protein is controlled by a particulate fraction rather than supernatant enzymes.
We wish to thank Mr. K. Noguchi of the Ex-perimental Sericultural Station of Miyagi for kindly supplying the silkworms for this study and also Mr. K. Otomo in this laboratory for his valuable assistance in feeding the silkworms.抄録全体を表示PDF形式でダウンロード (380K) -
SHUNZI MIZUHARA, TAKAHIRO KUWAKI, TOSHIHIKO UBUKA, GEORGE W. FRIMPTER1962 年 52 巻 1 号 p. 59-60
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (118K) -
TAKASHI HASHIMOTO, HARUHISA YOSHIKAWA1962 年 52 巻 1 号 p. 61-62
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (155K) -
ATSUSHI KIMURA, KOH-ITI TURUMI1962 年 52 巻 1 号 p. 63-65
発行日: 1962年
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (190K)
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