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Volume 47 (1960)
- Issue 6 Pages 699-
- Issue 5 Pages 559-
- Issue 4 Pages 401-
- Issue 3 Pages 273-
- Issue 2 Pages 145-
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Volume 47, Issue 4
Displaying 1-17 of 17 articles from this issue
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IV. EFFECT OF METALLIC IONS, VARIOUS NUCLEOTIDES AND THIAMINE DERIVATIVES ON THIAMINOKINASE FROM RAT LIVERYOSHITAKE MANO, RYO TANAKA1960 Volume 47 Issue 4 Pages 401-413
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe effects of metallic ions, thiamine derivatives as a phosphate acceptor, and nucleotides as a phosphate donor on rat liver thiaminokinase were investigated and the results were as follows.
1. Metallic ions effective as essential activator were Mg++, Mn++, Co++ and Ni++ among those tested. These ions had definite molar optimal relations to nucleotides used under the condition tested, but they were variable. Mg++ and Mn++ were in mutual antagonism to the activity. Ca++ and Zn++ acted as inhibitor.
2. Various thiamine derivatives except ethylthiamine could not be a substrate for the formation of cocarboxylase by the purified enzyme. Among the derivatives tested, disulfide compounds and ester derivatives of thiamine could serve as a substrate in the crude enzyme, and all of them may be considered to be induced to TDP via thiamine. Ethylthiamine was still active in the purest preparation. Ethylthiamine, butylthiamine and neo-pyrithiamine acted as an inhibitor competitive with thiamine.
3. Nucleotides as pyrophosphate donor were confined to ATP and UTP with the purified enzyme under the condition studied, and other nucleosides triphosphates could act as a substrate only with the crude system presumably by the action of other enzymes deriving them to the effective nucleotides. The activity with the effective nucleotides varied markedly with the reaction condition, such as pH and metallic ion concentrations. Moreover, all the nucleotides tested interacted inhibitorily with ATP upon the activity.
The authors wish to express their sincere thanks to Prof. N. Shimazono for his kind guidance.View full abstractDownload PDF (821K) -
III. ON THE PATHWAY OF PYRUVATE FORMATION IN BREVIBACTERIUM FLAVUM NO. 2247ISAMU SHIIO, SHIN-ICHIRO ÔTSUKA, TOSHINAO TSUNODA1960 Volume 47 Issue 4 Pages 414-421
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Labelled pyruvic acid was produced from glucose-l-, 6-, and U-C14 in the presence of arsenite by washed cell suspensions of Brevibacterium flavum No. 2247. The relative specific activities of pyruvate to the substrate glucose were; 0.449, 0.510, and 0.502, and the percentage of counts in carboxyl group of pyruvate were; 3.72, 1.41, and 33.95 per cent, for the substrates, glucose-l-, 6-, and U-C14, respectively.
2. From these results it was concluded that glucose was metabolized aerobically by both the Embden-Meyerhof and hexosemonophosphate oxidative pathway in the approximate ratio of 90:10.
The authors are indebted to Prof. S. Akabori of the Osaka University, Dr. T. Yamada of the University of Tokyo, and Dr, H. Oeda and Mr. N. Motozaki of our laboratory for the helpful discussion and encouragement during the course of this work.View full abstractDownload PDF (494K) -
XXXVII. MOLECULAR SIZE AND SHAPE OF PAROTINYOSOJI ITO, YUKIHO KUBOTA, YASUYO SHIBUYA1960 Volume 47 Issue 4 Pages 422-428
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe molecular size and shape of parotin were investigated by sedimen-tation, diffusion and viscosity measurements, and the following results were obtained.
1. The molecular weight of parotin was determined to be 132, 000 from the sedimentation coefficient (3.81×10-13), diffusion coefficient (2.84×10-7) and intrinsic viscosity (0.428), assuming the molecule to be a prolate ellipsoid with scarce hydration.
2. The frictional ratio and the corresponding axial ratio of the molecule were calculated to be 2.21 and 25.7, respectively. From these data, the molecular dimensions were evaluated to be 592Å×23Å.View full abstractDownload PDF (1095K) -
II. COMPARISON OF THE CHROMATOGRAMS OBTAINED WITH VARIOUS TISSUES INCLUDING TUMORSSHIGEO HORIE1960 Volume 47 Issue 4 Pages 429-444
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Using a modified semi-micro gradient elution chromatography, the distribution of the acid-soluble nucleotides in various normal and neoplastic tissues of rats was compared and the variations of the distribution were described.
2. The distribution and phosphate-turnover of the acid-soluble phosphorus compounds were also studied by intraperitoneal injection of P32 followed by the chromatographic analysis. The distribution patterns of nucleotides and radioactivity in liver, muscle, heart, lung, thymus, spleen, testicles, brain, fetal liver and experimental hepatomas were illustrated and the differences between these tissues were pointed out.
3. The characteristics of the experimental hepatoma tissue as compared with the normal liver tissue were as follows: a) The concentration of oxidized DPN was low. b) The incorporation of P32 inorganic phosphate into glucose-6-phosphate and L-α-glycerophosphate was absent or, if any, very low. c) Per cent of radioactivity of inorganic phosphate in the total acid-soluble radioactivity was extraordinary high as compared with other tissues as well as the liver tissue.
The author is deeply indebted to Prof. N. Shimazono for his kind advice and encouragement.View full abstractDownload PDF (878K) -
I. OXIDATIVE PHOSPHORYLATION BY MITOCHONDRIA FROM ASPERGILLUS ORYZAEKOZO IWASA1960 Volume 47 Issue 4 Pages 445-453
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Mitochondria prepared from aerated mycelia of Aspergillus oryzae in 0.5M sucrose containing 0.01M EDTA catalyzed the phosphorylation coupled with oxidation of succinate.
2. The phosphorylative activity was stabilized by addition of K-citrate.
3. High concentration of iP and hexokinase in the reaction mixture increased the phosphorylative activity. Addition of iP increased oxidation but hexokinase did not.
4. The oxidative phosphorylation had two pH optima at pH 6.3 and 7.0.
5. Addition of a nucleotide complex prepared from the organism and of DPN stimulated oxidative phosphorylation (as judged by the P/O ratio).
6. The inhibitory effect of antimycin A and 2, 4-DNP was studied. Antimycin A-insensitive oxidation of this preparation was very small and the phosphorylation mechanism, is tightly coupled with oxidation.
The author wishes to express his thanks to Prof. K. Okunuki for his valuable guidance. Thanks are also due to his colleagues Mr. T. Higashiyama of the same laboratory, and Dr. F. Imamoto of the laboratory of pharmacology, faculty of medicine, Osaka University, for their help and discussion.View full abstractDownload PDF (460K) -
TSUNEO OKUYAMA, KAZUO SATAKE1960 Volume 47 Issue 4 Pages 454-466
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Amino acids and lower peptides could be TNP-lated both with CITNB and with TNBS.
2. TNBS coupled with primary amino group but not with water nor other groups commonly encountered in protein, in water solution at pH 8. and at room temperature.
3. The preparation and some properties such as m. p., Rf, molar extinc-tion coefficient, photo-and acid-stabilities, of TNP-amino acids and -peptides. (α-mono-TNP-Gly, -L-Ala, -L-Val, -L-Leu, -L-Tyr, -L-Arg, -L-Asp, -L-Glu, L-Met, -L-His, ε-mono-and α, ε-Bis-TNP-Lys; α-mono-TNP-Gly-Gly, -Gly-DL-Val, Gly-DL-Ser, -DL-Ala-DL-AspNH2 and -L-Leu-L-Tyr) are reported, together with the ultraviolet and infrared absorption spectra of some typical TNP derivatives.
4. These results were briefly discussed with connection of possible application of TNBS in protein chemistry.
We are greatly indebted to Mrs. S. Sasakawa, Mr. H. Ozawa and Mr. T. Take, for their unpublished data. We wish to express our gratitude to Mr. K. Nitta, Mr. M. Ohashi, Mr. H. Shino and Mr. T. Shinoda for their technical assistance in the preparation of various TNP compounds.
These studies were supported in part by a grant from the Scientific Research Fund of the Ministry of Education. The authors should express their sincere thanks to them.View full abstractDownload PDF (835K) -
I. THE ADENOSINE TRIPHOSPHATE-PHOSPHATE EXCHANGE REACTION DURING OXIDATIVE PHOSPHORYLATIONKOZO IWASA1960 Volume 47 Issue 4 Pages 467-474
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The ATP-iP exchange reaction was studied in mitochondria. The exchange reaction was observed in a system with ADP as iP-acceptor and a hexokinase-glucose system as ATP-trapper due to the adenylate kinase in the mitochondria.
2. With succinate as substrate the exchange reaction was suppressed during oxidative phosphorylation as compared with substrates which presu-mably did not support electron transport.
3. The exchange reaction was inhibited by some specific inhibitors of oxidative phosphorylation, but not ascorbate, ferrocyanide or ferricyanide.
The author wishes to express his gratitude to Prof. K. Okunuki for his guidance. He would like to thank his colleagues Dr. F. Imamoto (Pharmacological Laboratory, Faculty of Medicine, Osaka University) and Mr. T. Higashiyama of the same laboratory for helpful discussion during this work.View full abstractDownload PDF (447K) -
XLIV. MOLECULAR WEIGHT OF SALIVA-PAROTIN-AYOSOJI ITO, YUKIHO KUBOTA1960 Volume 47 Issue 4 Pages 475-481
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe molecular weight of saliva-parotin-A was computed to be 15, 900, based on a sedimentation coefficient of 1.51×10-13 and a diffusion coefficient of 7.41×10-7. The molecular weight determined during the approach to sedimentation equilibrium was 15, 700. These values were shown to be con-sistent with the minimal molecular weight calculated from the amino acid composition.
This work was supported in part by the Grant-in-Aid for Scientific Research from the Ministry of Education to which the authors' thanks are due.View full abstractDownload PDF (2066K) -
SEIICHI HINO1960 Volume 47 Issue 4 Pages 482-494
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The effect of molecular nitrogen and several other nitrogenous com-pounds on the evolution of molecular hydrogen was studied using cell suspensions of a facultative aerobic bacterium, which closely resembles Bacillus polymyxa and fixes nitrogen only under anaerobic condition.
2. The organism produces hydrogen from sucrose, glucose, fructose, pyruvate and formate. No hydrogen is produced from several other substances such as fructose-diphosphate, gluconate, lactate or hypoxanthine.
3. The rate of hydrogen evolution from glucose or pyruvate gradually increases with time, while the rate of evolution from formate remains on a constant low level. Hydrogen or oxygen inhibits the hydrogen evolution from these three substrates to a similar extent.
4. Molecular nitrogen has a dual effect on the hydrogen evolution from glucose; initial inhibition followed by a remarkable stimulation. Under the condition in which the inhibitory effect of molecular nitrogen could clearly be demonstrated, ammonium salts, glutamate and several other amino acids did not show any such inhibition.
5. No initial inhibition by molecular nitrogen could be demonstrated on the hydrogen evolution from pyruvate or formate, although the stimulating effect of nitrogen could be observed with pyruvate. Ammonia also showed the stimulating effect on the hydrogen evolution from glucose and pyruvate.
The author wishes to express his sincere gratitude to Prof. T. Mori for his con-tinuous encouragement and advices. He is also grateful to Mr. S. Hiai for his valuable discussions. The expences for this work were partly defrayed by the Grant in Aid for the Scientific Research from the Ministry of Education.View full abstractDownload PDF (746K) -
S. S. TATE, C. V. RAMAKRISHNAN, N. T. PATEL1960 Volume 47 Issue 4 Pages 495-504
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe enzyme, acetyl Coenzyme A deacylase, has been detected and purified from cell free extracts of lime fruit tissue during the initial stages of their development. This enzyme is found to require magnesium for maximal activity. The possible role of this enzyme in citrate metabolism has been considered.
The authors' thanks are due to Dr. R. Rajalakshmi for guidance in the presenta-tion of this paper.View full abstractDownload PDF (409K) -
YUICHI YAMAMURA, ATSUSHI TANAKA, MASAHIKO KATO1960 Volume 47 Issue 4 Pages 505-512
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The conjugates of mycolic acid and several kinds of amino acid (leucine, valine, alanine, and phenylalanine) were synthesized.
2. The biological activities of the synthesized mycoloylamino acid were tested and it was shown that the activity of succinic dehydrogenase of mice liver was decreased 24 hours after the intraperitoneal injection of 0.1mg. of mycoloylleucine, mycoloylvaline, and mycoloylalanine, while the same dosis of free mycolic acid and mycoloylphenylalanine were without effect.
Support of this work by a grant of the Ministry of Education of Japan is gratefully acknowledged.View full abstractDownload PDF (473K) -
ICHIRO HARUNA, SHIRO AKABORI1960 Volume 47 Issue 4 Pages 513-527
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A procedure for the determination of C-terminal peptides and acidic amino acid containing peptides of proteins by means of partial hydrazinolysis was described.
2. Thirty five acidic DNP-peptide derivatives were isolated from a partial hydrazinolysate of ovalbumin and their N-terminal residues and amino acid compositions were analysed.
3. That the C-terminal part of the protein has the sequence, Val-Ser-Pro, was confirmed.
4. It was suggested that the peptide chain in protein is apt to be split at the N-sites of acidic amino acids by hydrazinolysis.
The authors wish to express their gratitudes to Dr. K. Ohno for his helpful advice through this investigation.View full abstractDownload PDF (926K) -
TSURU WADA1960 Volume 47 Issue 4 Pages 528-536
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. p-Phenylazobenzoyl Taka-amylase A is antigenic and gives rise to antisera when injected into rabbits in repeated doses.
2. It was demonstrated from the serological studies of antisera that there is an apparent cross reaction between Taka-amylase A and p-phenylazobenzoyl Taka-amylase and protease-modified p-phenylazobenzoyl Taka-amylase A.
3. Amylase- and maltosidase-activities of PAB-TAA and M-PAB-TAA were inhibited by antisera against PAB-TAA and TAA.
4. It was found that PAB protected PAB-TAA and M-PAB-TAA from the inhibition by its antiserum but no protection of PAB against the neutralization by anti-TAA was observed.
5. The results were consistent with the suggestion of Ikenaka that the enzymatically active sites and PAB-residue located close together on the enzyme molecule.
The author is indebted to Prof. S. Akabori of the Institute for Protein Research, Osaka University and to Prof. B. Maruo and Dr. H. Takahashi, the Institute of Applied Microbiology, University of Tokyo, for their kind help and criticism through out the investigation, and to Prof. T. Ogata for his helpful advice, especially on the immunological techniques. The author's thank should also go to Mr. S. Matsubara and Miss. H. Toda who kindly supplied purified PAB-TAA and M-PAB-TAA with α-phenylmaltoside.View full abstractDownload PDF (1360K) -
I. EFFECTS OF CALCIUM AND pH ON THE DENATURATIONSHIZUE FUJITA-IKEDA, TOSHIZO ISEMURA1960 Volume 47 Issue 4 Pages 537-547
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The effects of calcium and pH on the urea denaturation of taka-amylase A were investigated by the measurement of solution viscosity. The viscosity of solution increased with time after the protein was mixed with urea, and, in some condition, reached a steady value.
2. The rate of denaturation was markedly affected by the conditions of dialysis, even without ethylenediamine tetraacetic acid, i.e., by the amount of bound calcium which was not essential to maintain the active structure of the protein molecule. The increasing rate of viscosity was smaller as the content of bound calcium was higher. It seems that bound calcium play a role in stabilizing the secondary or tertiary structure of the molecule and inhibiting the molecular chain from unfolding itself.
3. When the amount of bound calcium was less than a certain definite one, taka-amylase A denatured in urea was hydrolysed by a trace of con-taminant, taka-protease. This implies that the proteolytic degradation of taka-amylase A is inhibited by bound calcium.
4. Taka-amylase A had its maximum stability towards urea denaturation near pH 6 to 7.View full abstractDownload PDF (606K) -
TOSHIZO ISEMURA, KINJI KAKIUCHI, HACHIRO ETO1960 Volume 47 Issue 4 Pages 548-550
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (1027K) -
I. INCORPORATION OF GLYCINE-C14 INTO PARTICLES OF POSTERIOR SILKGLAND IN VITROIWAO SUZUKA, KENSUKE SHIMURA1960 Volume 47 Issue 4 Pages 551-554
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (204K) -
II. INCORPORATION OF SPECIFIC C14-LABELED AMINO ACIDS INTO PROTEIN OF POSTERIOR SILKGLAND IN VITROIWAO SUZUKA, KENSUKE SHIMURA1960 Volume 47 Issue 4 Pages 555-557
Published: April 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (164K)
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