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Volume 46 (1959)
- Issue 6 Pages 669-
- Issue 5 Pages 535-
- Issue 4 Pages 397-
- Issue 3 Pages 219-
- Issue 2 Pages 107-
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Volume 46, Issue 2
Displaying 1-15 of 15 articles from this issue
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VI. PHOSPHOPEPTIDES FROM A BACTERIAL PROTEINASE INHIBITED BY DIISOPROPYL FLUOROPHOSPHATEHIROSHI MATSUBARA1959 Volume 46 Issue 2 Pages 107-112
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe phosphorus content of a bacterial proteinase, BPN', which had been inhibited by DFP, was analyzed and the site of attachment of the phosphorus, and structure of the adjacent peptide examined. One mole of phosphorus was present per mole of protein. It was shown that Ser must be the amino acid residue binding the phosphorus of DFP. The neighboring peptide con-tained Gly, Glu or Glu(NH2), and some other amino acids.
The author wishes to express his thanks to Prof. K. O kunuki and Dr. B. Hagihara for their kind advice during this work. I would like to thank Dr. M. L. Huggins, Research Lab., Eastman Kodak Co., Rochester, N. Y., for a gift of p-Semidine, and I am grateful to Nagase Co. Ltd. for kindly supplying the enzyme source materials.View full abstractDownload PDF (288K) -
KOZO IWASA, FUMIO IMAMOTO, KAZUO OKUNUKI1959 Volume 46 Issue 2 Pages 113-120
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Mitochondrial fractions of Aspergillus oryzae prepared in sucrose possess ATP-ase activity and the activity increased buring incubation at 30°. This increase was stimulated by addition of magesium and calcium.
2. Apparent ATP-ase activity of the mitochondrial fraction showed a two steps curve, the second probably resulting from the combined action of adenylate kinase and ATP-ase.
3. ATP-ase of the soluble fraction is also activated by magnesium, inhibited by calcium, and gives a two steps curve like the mitochondrial fraction.
4. During ageing of the mitochondrial fraction, ATP-ase is liberated from the particles into the medium.
The authors wish to express their gratitude to the Ministry of Education for a Grant in Aid for Fundamental Scientific Research.View full abstractDownload PDF (350K) -
III. DETERMINATION OF “NATIVE” MAMMALIAN HEART MUSCLE CYTOCHROME C AND ITS PHYSIOLOGICAL PROPERTIESTATEO YAMANAKA, HIROSHI MIZUSHIMA, MITSUHIRO NOZAKI, TAKEKAZU HORIO, K ...1959 Volume 46 Issue 2 Pages 121-132
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn order to determine “native” cytochrome c, cytochrome c was purified from bovine, horse and pig heart muscle by the various treatment involving both mild and drastic procedures and some physiological properties of the resulting cytochrome c's were compared.
In comparison with the modified cytochrome c's, the most native form of cytochrome c has the lowest ascorbate-oxidizing activity is the least susceptible to digestions by bacterial proteinase and trypsin and has the least affinity for Amberlite XE-64.
Both the native and modified forms are reduced to almost the same extent by yeast lactic dehydrogenase and have the same absorption spectrum in their oxidized and dithionite-reduced forms. Native cytochrome c can be easily crystallized. Crystalline mammalian cytochrome c's are easily digested in their oxidized form by bacterial proteinase, but hardly attacked in their reduced form, indicating that oxidation and reduction of the heme-moiety accompanies a definite change in the protein-moiety of the cytochrome c.
From the properties of the isolated forms of cytochrome c, the state of functional cytochrome c in living cells is discussed.
The authors wish to express their thanks to Messrs. T. Higashi and J. Yamashita for their help and discussion during this investigation.View full abstractDownload PDF (555K) -
II. QUANTITATIVE ANALYSIS OF THE COMPONENT AMINO ACIDS AND GLUCOSAMINE BY MEANS OF COLUMN CHROMATOGRAPHYHANAKO YOKOI1959 Volume 46 Issue 2 Pages 133-139
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSQuantitative analysis for the amino acids and glucosamine assumed to occur as sugar-polypeptide complex in alkaligenic acid was conducted following the method by Moore and Stein with slight modification. It has been evidenced that glucosamine as well as ten amino acids including aspartic acid, serine, glutamic acid, glycine, alanine, valine, isoleucine, leucine, phenylalanine and lysine are present in an approximately equimolar pro-portion with the exception that glutamic acid exists to a higher and alanine to a lower extent. In addition, an unidentified ninhydrin positive substance was found as a sharp peak appearing ahead of the aspartic acid peak in the chromatographic pattern.
The auther wishes to express her gratefulness to Prof. Akashi for his kind encouragement and advice throughout this investigation.View full abstractDownload PDF (281K) -
FUMIO IMAMOTO, KOZO IWASA, KAZUO OKUNUKI1959 Volume 46 Issue 2 Pages 141-150
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Mitochondria isolated from mycelia of Aspergillus orytiae catalyzed the oxidation of exogenous DPNH and components of TCA-cycle. These oxidations were carried out through cytochrome c, which was observed in mitochondria with a hand-spectroscope.
2. Contrary to the current conception, it was not demonstrated that external cytochrome c and DPN are essential for the oxidation of pyruvate in the case of mitochondria of Asp. orytiae. However, 2, 6-dichlorophenol indophenol was reduced rapidly in the presence of pyruvate. The oxidation of pyruvate by mitochondria was strongly stimulated rather than being inhibited by 10-3M cyanide.
3. DPNH oxidation was stimulated by EDTA and by a low concentra-tion of cyanide. It is concluded from these results that the stimulation is accompanied by chelation of some cations which may be bound to the particles and normally maintain a low rate of oxidation.
4. Fe++ and Fe+++ ions inhibited the oxidation of DPNH strongly and their inhibition was reversed by addition of either cyanide at the low concentration or of EDTA.
5. The properties of the mitochondria were compared with those of particles and the soluble fraction.View full abstractDownload PDF (415K) -
IV. TREATMENT WITH CARBOXYPEPTIDASE AND AMINOPEPTIDASEKOITI TITANI, HISAYUKI ISHIKURA1959 Volume 46 Issue 2 Pages 151-154
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSMore than seven moles of amino acids were liberated from the C-terminal of cytochrome c by the treatment with carboxypeptidase. The catalytic activity of the protein in a succinic oxidase system was retained through out the course of digestion.
Leucine aminopeptidase prepared from swine kidney did not split N-terminal amino acid from native cytochrome c.
Authors express their thanks to Prof. S. Akabori and Prof. H. Yoshika wa for constant guidances in the course of the work. Thanks are also due to Mr. Y. Nagai and Mr. Tobita of the Institute of Science and Technology, University of Tokyo for the generous gift of leucine aminopeptidase and carboxypeptidase used in the preliminary experiments.View full abstractDownload PDF (178K) -
TATSUYA SAMEJIMA1959 Volume 46 Issue 2 Pages 155-159
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The process of alkali denaturation of bovine liver catalase was investigated by following the changes of sedimentation pattern and enzyme activity of the solutions under various pH conditions from 7.0 to 12.0. It was found that the catalase molecule is split by alkali into homogeneous components having a sedimentation constant of 3.1S. The splitting pro-ceeded to completion at pH 12.0, where also the enzyme activity disappeared completely.
2. The molecular weight and axial ratio of the split component as determined by the observation of sedimentation and diffusion constants were computed to be 85, 000 and 1.8, respectively. Comparing these values to those of native catalase, it was deduced that the catalase molecule is composed of three particles of the 3.1 S component, connected lengthwise to form a rod-shaped molecule.
3. When the alkali-treated catalase solution was neutralized (to pH 7.0), the catalase activity recovered partially, and two peaks appeared in the sedimentation pattern. The sedimentation constant for one peak agreed with that of native catalase and the constant for the other peak suggested the existence of a dimer of the 3.1S component.
The author wishes to express his sincere gratitude to Prof. K. Shibata and Dr. M. Nagahisa for their kind guidance and encouragement and also to Prof. H. Tamiya for his many suggestions and advices in preparing this manuscript.View full abstractDownload PDF (196K) -
SUSUMU NISHIMURA, MASAYASU NOMURA1959 Volume 46 Issue 2 Pages 161-167
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. RNase of B. subtilis was accumulated in the culture medium as an exoenzyme. RNase production varied markedly with conditions of culture, phases of growth and strains.
2. Two types of RNases of B. subtilis were separated by column chroma-tography using the carboxylic acid cation exchange resin IRC-50 (XE-64).
3. By employing the acid treatment, ammonium sulfate fractionation and column chromatography, one of the enzymes was purified almost 400 fold. Its specific activity was comparable to that of crystalline pancreatic RNase.
4. Properties of RNase were reported,View full abstractDownload PDF (276K) -
HISATO YOSHIMURA, TERUO ASADA, MASAO IWANAMI1959 Volume 46 Issue 2 Pages 169-176
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDissociation exponents of uric acid and creatinine (at 37°) were estimated by aid of Shima's formula, and following results were obtained.
1. Effects of formaldehyde upon the first acid dissociation exponent of uric acid in 6mM solution, pKF', was derived from Levy's equation, and the following formula was obtained.
pKF'=5.08-log(1+8.198F), where F is molar concentration of formaldehyde (below 0.26M).
2. With a series of uric acid solutions of 1.5mM, in which 0.04 per cent formaldehyde and various amounts of NaCl up to 1M were contained, effects of ionic strength, μ, upon the dissociation exponent, pK', were examined, and the following equation was obtained.
pK'=5.13-0.5√μ-t+0.082μ
3. From the above two equations, the thermodynamic dissociation exponent of uric acid which has neither formalin effect nor salt effect is calculated to be 5.165 at 37°.
4. The base dissociation exponent phb' of creatinine in solutions of various ionic strength (below 0.4M) is expressed by the following equation.
pKw-pKb'=4.75+0.5√μ-0.43μ, where pKw is the dissociation exponent of water. The thermodynamic dissociation exponent of creatinine is thus calculated to be 8.76at 37°.
A part of the expense of this research was defrayed by aglant from the Department of Education to whom hte authors' thanks are due.View full abstractDownload PDF (294K) -
I. DINITROPHENYLATION OF TAKA-AMYLASE ATOKUJI IKENAKA1959 Volume 46 Issue 2 Pages 177-183
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Fluorodinitrobenzene was reacted with Taka-amylase A. The amylase activity seems to be completely lost when 2 moles of tyrosine and 5 moles of lysine residues are dinitrophenylated by the reagent.
2. When dinitrobenzene sulfonate was reacted with Taka-amylase A at pH 10.7, 11 out of the total 22 lysine residues in the amylase molecule were dinitrophenylated. About 60 per cent of the original activity was still remained under these conditions.
3. It was suggested that ε-amino groups of lysine residues may not be essential for the amylase activity but some special phenolic groups of tyrosine may be more closely connected to the activity.
The author wishes to express his gratitude to Prof. S. Akabori for his kind guidance throughout the investigation and to Mr. Usami for his technical assistance, and also to the Sankyo Co. Ltd. for their kind supply of “Takadiastase Sankyo”.View full abstractDownload PDF (269K) -
SHUNJI OUCHI, ATSUSHI TANAKA, NOBUO IZUMIYA1959 Volume 46 Issue 2 Pages 185-188
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe improved method of synthesis of L-cysteic acid amide has been established, which utilizes the following reactions: (I) conversion of cysteic acid to cysteic acid ethyl ester; (2) amidation of the ester to yield cysteic acid amide.
Partially purified leucine aminopeptidase hydrolyzes cysteic acid amide at 0.11 per cent and 0.083 per cent at 0.025M and 0.01M substrate con-centrations, respectively, of the rate of L-leucinamide.
The authors wish to thank Prof. S. Shibuya for his interest in this study.View full abstractDownload PDF (169K) -
MITSUO TORII1959 Volume 46 Issue 2 Pages 189-200
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSGlutamyl polypeptides by B. anthracis, B. megateriutn and B. subtilis were subjected to hydrazinolysis in order to elucidate the form of linkage of these polypeptides. Hydrazinolysis of these peptides at 100° gave not only glutamic acid γ-hydrazide but also considerable amounts of glutamic acid αγ-dihydrazide and pyrrolidone carboxylic acid hydrazide which seemed to be secondary products. When prolonged hydrazinolysis was carried out at low temperature, the amount of γ-H increased, while those of αγ- and p-H decreased. On hydrazinolysis at 37° for 50 days, major products were γ-H (52-55 per cent) and PCA (29 per cent) which was derived from γ-H. α-Hydrazide was not found in all experiments. These facts suggest that these glutamyl polypeptides are almost solely composed of γ-linkage. The anthor wishes to acknowledge the valuable advice and encouragement of Prof. T. Amano (Department of Bacteriology, Osaka University Medical School), Prof. S. Akabori (Department of Chemistry, Osaka University), Dr. K. Ohno (Ajinomoto Co., Inc.) and Dr. K. Narita (Ochanomizu Women's University)View full abstractDownload PDF (478K) -
SATORU MAKISUMI1959 Volume 46 Issue 2 Pages 201-205
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFor confirming the proposed structure of desaminocanavanine, the com-pound was subjected to the catalytic hydrogenolysis with palladium charcoal and hydrogen gas in expectation of the cleavage at O-N bond. The hydrogenolysis product of desaminocanavanine, N-amidinohomoserine (a-guanidino-γ-hydroxybutyric acid), was isolated. Its characterization and identification were carried out by elementary analysis, anhydride formation, alkaline hydrolysis to homoserine and ammonia, and synthesis from homoserine.
From the fact that the hydrogenolysis product is only N-amidinoho-moserine, the provisional cyclic formula of desaminocanavanine was found to be true.
The author wishes to thank Prof. S. Shibuya for his valuable advice.
This work was supported in part by a Grant in Aid for the Miscellaneous Scientific Research from the Ministry of Education.View full abstractDownload PDF (228K) -
NIKICHI OKUMURA, SABURO OTSUKI, TATSUYA AOYAMA1959 Volume 46 Issue 2 Pages 207-212
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Comparative studies on free amino acids and their related compounds in the brains of various animals have been done by the methods of ion-ex-change chromatographies.
2. The animals examined were the catfish, frog, tortoise, hen, and rat. The frog and tortoise were in hibernation.
3. The large differences were observed in the cold-blooded animals in comparison with the warm-blooded animals. Especially, lower values of glutamic acid, aspartic acid, alanine, serine and N-acetylaspartic acid were found in cold-blooded animals than in the warm-blooded. Unidentified substance X2 containing threonine, phosphoric ester and other ninhydrin positive substances was found in a very large amount in the brains of the catfish, frog and tortoise.
4. The amount of γ-aminobutyric acid was much the same in all the vertebrates examined.
5. Extremely small amounts of taurine were obtained in the frog and tortoise, both in hibernation.
6. Some of other amino acids and related compounds were found in different amounts in the brains of animals of different species.View full abstractDownload PDF (247K) -
TAMITARO MIZUNOYA1959 Volume 46 Issue 2 Pages 213-218
Published: February 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe author surveys the various suggestions presented from the ther-modynamical viewpoint concerning the criteria of biological evolution (Section I).
As a thermodynamical criterion for the judgement of the primitiveness of metabolic pathways, an approximate equation for the dissipation rate T_??_ of the available energy of the metabolizing system:
T_??_=(ΔG-W)/T is proposed, where ΔG is the difference of Gibbs' free energy between the initial reactants and the final products of the metabolic process, W the work done by the system and r is the time required for the one process. From this criterion, that of Oparin and that of Odum and Pinkerton are derived as two special cases, respectively. The third special case leads us to a suggestion that organisms have probably proceeded towards the direction of a longer period of the metabolic process, from which the gain of new reaction steps and the complication of the metabolic patterns are derived (Section II).
The primitiveness of the tri- and dicarboxylic acid cycles, which can not be inferred from the Oparin's criterion, is discussed as a good ex-ample of the last case (Section III).View full abstractDownload PDF (319K)
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