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Volume 42 (1955)
- Issue 6 Pages 615-
- Issue 5 Pages 449-
- Issue 4 Pages 367-
- Issue 3 Pages 221-
- Issue 2 Pages 99-
- Issue 1 Pages 1-
Volume 42, Issue 6
Displaying 1-27 of 27 articles from this issue
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III. ON THE CARBOXYL-TERMINAL PEPTIDEKO OHNO1955 Volume 42 Issue 6 Pages 615-625
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A new procedure for determining the amino acid sequences from carboxyl-terminal of proteins by means of hydrazinolysis was described.
2. Asparaginyl (or aspartyl)-glycyl-alanyl-asparaginyl-leucine was proposed as carboxyl terminal peptide of lysozyme.
The author wishes to express his deep thanks to Prof. Shiro Akabori for his interest and encouragements throughout this investigation.View full abstractDownload PDF (736K) -
I. ON THE THIOL GROUPS OF THE NUCLEOPROTEINS OF RABBIT LIVERTADAMOTO NISHIYAMA1955 Volume 42 Issue 6 Pages 627-632
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Majority of the nucleoproteins isolated from rabbit liver by the method of Greenstein et al. was RN-protein.
2. Almost all of its thiol groups were freely reacting. The mean ratio of the freely reacting thiol groups to the total thiol groups of RN-protein was 85.5 per cent, while that to the DN-protein was 34.8 per cent.
3. The protein moiety of DN-protein may by considered to be a histone-like protein and 36.3 per cent of its total thiol groups was freely reacting.
4. The protein moiety of RN-protein may be neutral or acid protein, and all of its thiol groups were freely reacting.
The author wishes to his gratitude to Prof. J. Hirade and Dr. T. Shimizu for their advices and encouragement in this research.View full abstractDownload PDF (300K) -
II. ACTIVATION OF PROTEINS BY NUCLEIC ACIDSTAIJI SHIMIZU, TADAMOTO NISHIYAMA1955 Volume 42 Issue 6 Pages 633-640
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Free amino and thiol groups of various proteins increased when incubated with ribonucleic acid.
2. Ribonucleic acid increases free disulfide groups of serum al-bumin previously denatured by urea but not native serum albumin.
3. Alkylation velocity of the amino groups of various proteins with iodoacetaminde is accelerated remarkably by the addition of ribo-nucleic acid.
4. Ribonucleic acid decreases the viscosity of serum albumin and
ovalbumin. This shows that there is an interaction between these proteins and ribonucleic acid.
The authors express their deep gratitude to Prof. J. Hirade for his advice and kind guidance.View full abstractDownload PDF (354K) -
HITOSHI OZAWA, KAZUO SATAKE1955 Volume 42 Issue 6 Pages 641-648
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSN-terminal sequences of hemoglobin molecule from various animals were determined by the DNP- and PTH- methods and the following results were obtained:
Horse, pig Val-Leu- Val-Gly- Val-Glu-(Leu)
Dog Val-Leu- Val-Gly- Val-Asp-
Bovine, goat, sheep Val-Leu- Met-Gly Val-Asp-
Guinea pig Val-Leu- Val-Ser- Val-Asp-
Rabbit, snake Val-Leu- Val-Gly Val-Asp-
Hen Val-Leu- ? ?
We wish to express our gratitude to Prof. Akabori for his interest and encourage-ment through this work, and to Mr. K. Kusama, Mr. K. Titani, and Mr. H. Oku-yama for their technical assistance.View full abstractDownload PDF (465K) -
III. CHROMATOGRAPHIC STUDIES OF THE ACTIVATION OF α-CHYMOTRYPSINOGEN TO α-CHYMOTRYPSINNAOKAZU SAKOTA1955 Volume 42 Issue 6 Pages 649-655
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. α-Chymotrypsin could be effectively chromatographed on columns of Dowex-50 with 0.1M sodium citrate buffer of pH 6.77, while α-chymotrypsinogen with the same buffer of pH 5.5. The both proteins seem to be chromatographically homogeous, and not to be affected by the procedure.
2. The activation of α-chymotrypsinogen by trypsin was studied chromatographically. The zymogen and two active proteins were separated by the method, and one of the two active proteins seemed to be α-chymotrypsin accompanied with another highly active intermediate protein.
The author wishes to thank professor Shiro Akabori for his guidance through-out this work, and also Mr. Yoshimi 0kada for his valuable technical assistance.View full abstractDownload PDF (421K) -
I. THE EFFECTS OF IMIDAZOLE DERIVATIVES ON THE AUTOÖXIDATION OF L-ASCORBIC ACIDYUJIRO IMANAGA1955 Volume 42 Issue 6 Pages 657-667
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The effects of imidazole derivatives on the autoöxidation of L-ascorbic acid were studied.
At pH 7.1, imidazolecarboxylic acid was the most accelerative, while methylimidazole was the most depressive. These effects reversed at pH 4.3.
2. The ultraviolet absorption spectra of L-ascorbic acid-imidazole derivative-phosphate buffer system was measured, and the possibility of the complex formation between L-ascorbic acid and imidazole derivatives was examined.
3. The effects of these imidazole derivatives were also discussed as regards the differences in the contaminating Cu_??_ concentration.View full abstractDownload PDF (502K) -
II. THE DECOMPOSITION PRODUCTS OF IMIDAZOLE DERIVATIVES PRESENT IN THE AUTOOXIDATION MIXTUREYUJIRO IMANAGA1955 Volume 42 Issue 6 Pages 669-676
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The degradation of imidazole derivatives by aeration in the presence of L-ascorbic acid was studied. It was found that the amino acids formed have the structures corresponding to the starting imidazole derivatives.
2. While hydroxymethylimidazole was hardly attacked by H2O2, histidine is easily oxidized by H2O2 as well as by aeration in the presence of ascorbic acid. Aspartic acid was detected and isolated from the oxidation products. The effect of ascorbic acid cannot be attributed simply to the action of H2O2 secondarily formed in the autoöxidation.
3. The effects of imidazole derivatives on the autoöxidation of L-ascorbic acid (preceding paper) were discussed taking the reactivity as the chain breaker into account.
The author thanks Prof. S. Akabori, Osaka University and Prof. Y. Mats u-shima for their kind guidances. His thanks are also due to Mr. S. Sakurai, Osaka University, and Misses K. Konishi and N. Ishimoto for their technical assistance.View full abstractDownload PDF (442K) -
NOBUYOSHI SAKAI, EIJI SHIMOSATO1955 Volume 42 Issue 6 Pages 677-684
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Each component of the complement of guinea-pig's serum in which ascorbic acid was reduced remarkably by feeding with the diet deficient in ascorbic acid, or even of the serum of animals which were suffering from severe scurvy, remained without any reduction.
2. Addition of ascorbic acid to the serum of scorbutic guinea-pigs in vitro gave no change in the content of each component of the complement.
3. Lowering of ascorbic acid contents in the normal guinea-pig's serum by the addition of CuCl2 in vitro, resulted in no change in each of its component of the complement.
From these results it may be said that any component of complement has no relatin with ascorbic acid directly.
The authors wish to express their sincerest thanks to Prof. Shiro Fujimura for his kind directions in carrying out this work.View full abstractDownload PDF (500K) -
NOBUYOSHI SAKAI1955 Volume 42 Issue 6 Pages 685-698
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe effects of some cations and anions on the complementary ac-tion were investigated and following results were obtained.
Ca++, Ba++, Sr++, Mg++, SO4-- and H2PO4- inhibited the action of the complement and by removal of them, the activity of the complement could be restored.
The mechaism of the anticomplementary action of these ions was based neither on the destruction of each factor necessary to the hemolytic reaction, such as hemolysins, red corpuscles or components of complement, nor on the effects upon the combination of the hemolysins and red corpuscles.
The inhibitory action of these ions was due to their interference on the combination of each component of the complement with sensitized
corpuscles. Exceptionally, only HPO4-- did not inhibit the 4th component to combine with sensitized corpuscles.
These effects were shown to be caused only by the presence of the ions in the medium of the hemolytic system, but not by inactivation of complement due to the combination with ions. Even if the components due to the combination with ions. Even if the components of complement combine with them, the combination is probably reversible.
In conclusion the author wishes to express his hearty thanks to Prof. S. Fujimura for his kind guidance in this reserach.View full abstractDownload PDF (740K) -
NOBUKO SENO, KENICHIRO MURAI, KENSUKE SHIMURA1955 Volume 42 Issue 6 Pages 699-704
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The amino acid sequence in N-terminal lysylpeptides of α-casein has been investigated.
2. The di-DNP-lysylpeptides were separated by silicic acid-celite adsorption chromatography and by paper electrophoresis.
3. It was concluded that the N-terminal sequence is Lys-Leu-Val-Ala-Glu-Asp-.
The authors wish to express their gratitudes to Prof. T. Ando and Prof. H. Nishi-kawa for their guidance and encouragement and to Miss. R. Saeki for her technical assistance.View full abstractDownload PDF (332K) -
II. ON THE MECHANISM OF SURFACE DENATURATION OF LYSOZYMEKOZO HAMAGUCHI1955 Volume 42 Issue 6 Pages 705-714
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn order to clarify the mechanism of surface denaturation of lysozyme, the effects of the temperature of substrate and of the e-lapsed time before measurements on the F-A curves were studied. The results obtained were as follows:
(1) By plotting the areas at constant pressure against the tempera-tures of substrate, the points were found to be grouped into three curves, one of which was obtained from the solution in which lysozyme molecules were not denatured. The second, the curve was obtained from the solutions in which the protein molecules were denatured and the ac-cumulation of the points around this curve was independent of the denaturing agents. The third, the curve was obtained from the so-lutions in which the denaturation was rather drastic and on the water surface of which temperatures were sufficiently high.
(2) When native lysozyme molecules were spread on water sur-face, the surface denaturation was of a first order process. The activation of 15 kcal./mole was necessary for the surface denaturation of the globular molecules in adsorbed layer. This is the reason why the F-A curves of lysozyme were profoundly affected by the temperature of substrate and by the aging before measurements. It was suggested that this activation energy for the proteins which had been so far investiggated would be so small that the effects of temperature were not observed, and that to denature proteins in solutions beforehand plays a role of reducing this activation energy.
In conclusion, the author expresses his hearty thanks to Prof. T. Isemura for his kind guidance throughout the present work, and to Prof. S. Akabori and Mr. K. Ohno in Faculty of Science, Osaka University who kindly supplied the valuable sample to him.View full abstractDownload PDF (606K) -
MITUO EBATA, RYO SATO, TCHANGI BAK1955 Volume 42 Issue 6 Pages 715-725
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A phosphokinase catalyzing the phosphorylation of sedoheptulose with ATP was found in a cell-free extract of a Bacillus species, Strain W-2, grown in the presence of this sugar.
2. An equimolar relationship was observed between the disap-pearance of free heptose and the decrease of acid-labile phosphate in the phosphokinase reaction. This suggests that the reaction product is a sedoheptulose monophosphate.
3. The reaction products were isolated as crude barium salts which gave a spot corresponding to sedoheptulose on paper chromatogram after (but not before) hydrolysis by a phosphatase preparation.
4. The pH-activity curve of this enzyme has two maxima at pH 6.4 and 9.0.
5. The enzyme requires Mg++or Mn++for its activity, Mn++being less effective as activator.
6. NaF, NaN3, iodoacetate, Cu++, and alloxane are inhibitory to the enzyme. The inhibition by alloxane can be reversed by cysteine.
7. Several common hexoses and pentoses are inactive to the enzyme. They do not interfere with the phosphorylation of sedoheptulose.
The authors are indebted to Prof. T. Ishikawa and Dr. Y. Kurata of the Department of Pathology, Faculty of Medicine, Kanazawa University for their kindness in making their instruments available to the authors.View full abstractDownload PDF (631K) -
TAMIO YAMAKAWA, SHIZUE SUZUKI1955 Volume 42 Issue 6 Pages 727-736
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A substance giving purple color with Bial's reagent was isolated from serum mucoprotein in crystalline form and designated as ‘sero-lactaminic acid’.
FIG. 6. Serum hexosamine and sero-lactaminic acid in diseases
2. The nature of sero-lactaminic acid, lactaminic acid and N-acetyl-neuraminic acid is discussed comparatively.
3. By the chromatographic technique with cation exchanger, it is revealed only glucosamine and no chondrosamine was present as hexosamine constitutent of serum.
4. The contents of sero-lactaminic acid and glucosamine in various animal sera and a variety of patients sera were determined and the increases of both component were noticed in several pathological conditions.View full abstractDownload PDF (1257K) -
SHIGETOH MIYACHI, TOYOYASU HIROKAWA, HIROSHI TAMIYA1955 Volume 42 Issue 6 Pages 737-743
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The light-induced C14O2-fixing capacity of algal cells (Chlorella), as it was measured by the technique of Ca1vin et al. (2, 12), was found to be markedly decreased when quinone was added to the algal suspension.
2. The suppressing effect of quinone was reversible when its con-centration was low (10-4.3M or less), but became irreversible when the quinone concentration was raised (10-4M or more). The reversible suppression of C14O2-fixing capacity caused by quinone in lower con-centrations was explained as due to the reaction between the photo-chemically produced reducing substance and quinone, and the irreversibility of the quinone effect at its higher concentrations was inter-preted as being due to the irreversible destruction of the reaction system between the photochemically formed reducing substance and C14O2.
3. It was inferred that the Hill reaction brought about by quinone is nothing but a reaction between quinone and a reducing agent, whose photochemical formation in algal cells can be revealed by the measure-ment of light-induced C14O2-fixing capacity according to the method of Calvin et al.
This work was aided by grants from the Ministry of Education and the Rocke-feller Foundation. To these bodies we extend our grateful thanks. Our thanks are also due to Mr. Seikichi Izawa for help with some of the experiments.View full abstractDownload PDF (387K) -
TAKAO NAKAMURA1955 Volume 42 Issue 6 Pages 745-748
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (182K) -
SHIGEKI MINAKAMI1955 Volume 42 Issue 6 Pages 749-756
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Cytochrome c of baker's yeast was purified by ion exchange resin chromatography.
2. Absorption spectrum, oxidation-reduction potential, isoelectric point and enzymatic activities of both yeast and heart cytochrome c were closely similar.
3. Similar chromatograms and paper-elctrophoreses of both cyto-chrome c were obtained, but yeast cytochrome showed wider bands by chrmatography and diffuse boundaries by electrophoresis.
The author expresses his thanks to Prof. H. Yoshikawa and D. Y. Yoneyam a for constant guidances and Dr. M. Ishimoto, Department of Chemistry, Faculty of Science, and Dr. J. Koyama, Institute for Infectious Diseases, for their constant advices and encouragements in the course of the work. This work was aided by a grant from the scientific research fund of the Ministry of Education.View full abstractDownload PDF (406K) -
KUNIO YAGI, YOSHITAKA MATSUOKA1955 Volume 42 Issue 6 Pages 757-762
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFlavin compounds could be separated by virtue of different mobilities in the electrophoresis on the buffer-moistened filter paper. Each flavin was eluted with water, and their concentration was determined by measuring the light absorpion of the eluate at 450mμ or by the lumiflavin fluorescence method. The recovery by this method was satisfactory, being 100±5 per cent.View full abstractDownload PDF (289K) -
YUKIO YAMAMOTO1955 Volume 42 Issue 6 Pages 763-774
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Changes in content of ammonia-N, amino-N, glutamine amide-N, asparagine amide-N, and total soluble-N of each seed organ of Vigna sesquipedalis, i.e. plumule, epicotyl, hypocotyl, radicle, and cotyle-don were followed daily during the course of the germination stage.
2. Both amides and amino acids that disappeared from the cotyledon were apparently recovered as such in the growing tissues, in particular in the hypocotyl. The hypocotyl was able to produce asparagine newly from aspartate and ammonium salt; ATP added exerted an accelerating action on the synthesis.
3. From asparagine and -ketoglutarate added, a partially purified hypocotyl preparation produced glutamic acid and ammonia. It was suggested that in this α-keto acid dependent deamidation of asparagine in hypocotyl the asparaginase-transaminase and/or the Meister's transaminase-deamidase may be involved. Pyridoxamine phosphate functioned as a cofactor in this reaction.
4. In the stem tissues a parallelism between the asparagine level and the protein synthesis was seen.
The author is greatly indebted to Assist. Prof. Dr. Y. Oota for his instructive advices in the course of the study. Thanks are also due to Prof. Dr. T. Mori of this institute for his sustained interest.View full abstractDownload PDF (697K) -
SEIICHI HINO1955 Volume 42 Issue 6 Pages 775-784
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. With the cultures of a strain of Clostridium isolated from soil, the process of anaerobic fixation of molecular nitrogen as well as its inhibition by various substances was studied.
2. For the anaerobic N2-fixation to be maintained in its active condition during sufficiently long culture periods, cares must be taken to keep the pH of the medium as constant as possible.
3. The level of anaerobic N2-fixation thus achieved was usually as high as 90μg. N per ml. of the culture solution during the first 24 hours' incubation, a value almost comparable with those obtained by previous workers in aerobic fixation with Azotobacter.
4. Carbon monoxide and nitrous oxide were found to inhibit the anaerobic N2-fixation in a specific manner, in that they do not affect (N2O) or do inhibit only in less pronounced extent (CO) the assimilation of ammonium-N by the bacterium.
5. Cyanide, azide, monoiodoacetate, p-chloromercuribenzoate and o-phenanthroline were also found to be powerful inhibitors of the anaerobic process, though their action on the fixation system seemed to be unspecific in nature.
6. Based on these findings, some discussions were made on the mechanism of the biological N2-fications.
The writer wishes to express his sincere gratitude to Prof. T. Mori of this laboatory for his continuous encouragement and advices. Thanks are also due to Prof. H. Tamiya of the University of Tokyo and Dr. A. Takamiya of the Tokyo In-stitute of Technology for their valuable suggestions. The work was partly supported by the Grant in Aid for Scientific Research from the Ministry of Education.View full abstractDownload PDF (609K) -
YUICHI YAMAMURA, MASAMICHI KUSUNOSE, EMI KUSUNOSE1955 Volume 42 Issue 6 Pages 785-792
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe alumina ground extract of Mycobacterium avium catalyzes the coupled oxido-reduction as the following equation.
2 L-Malate→oxalacetate+succinate
(or fumarate)
This reaction is inhibited by neither malonate nor BAL. It is suggest-ed that this reaction plays a rôle in the metabolism of M. avium, since it proceeds considerably fast.
The authors wish to express their thanks to Prof. S. Watanabe, the chief of the Toneyama Institute for Tuberculosis, and Prof. S. Akabori, Faculty of Science, Osaka University, for their counsels and encouragements during this investigation.View full abstractDownload PDF (446K) -
I. SPECIFICITYEIZI ITO, SATOSHI KONDO, SHIZUO WATANABE1955 Volume 42 Issue 6 Pages 793-803
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (645K) -
I. ISOLATION OF β-ALANINE AS THE N-TERMINAL RESIDUE OF THE ACTIVE PEPTIDEISAKU KASUYA, AKIRA HAGITANI1955 Volume 42 Issue 6 Pages 805-816
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A basic tuberculin active protein has been isolated from heat-killed culture filtrate of tubercle bacilli (human strain), either by phosphotungstic acid precipitation or by caolin adsorption, the uniformity of which was ascertained by paper-electro-ionophoresis at pH 6.8 phosphate buffer.
2. Through performic acid degradation, this basic active protein is devided into two cysteic acid-containing peptides: viz. one acidic and one basic indicating that these two peptides were linked together with at least one -S-S- bridge.
3. Among the three peptides, only the basic and neutral one are tuberculin active, concerning which a detailed study has been made in this paper; while the acidic one, which is inactive, will be discussed in a subsequent paper.
4. The shortest active unit of these peptides, viz. the neutral one, seems to be derived from the basic one, is composed of β-alanine, glutamic acid, glycine, and cysteic acid. The N-terminal residue of this peptide identified as β-alanine by paperchromatography of DNP-derivative.
In conclusion a grateful acknowledgement is made for the financial aid of the Ministry of Education and of the Ministry of Welfare. The authors also offer their sincers thanks to Prof. C. Nishino the director of the 2nd. Tokyo National Hospital, for his valuable advice; and also to Mr. J. Goto for his assistance throughout in the chemical analyses and in the animal experiments.View full abstractDownload PDF (704K) -
YOSHISHIGE UMEBACHI, KIKUKO TSUCHITANI1955 Volume 42 Issue 6 Pages 817-824
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. An unidentified diazo-positive substance of the fruit-fly, D. melanogaster, was compared with synthetic xanthurenic acid in regard to the Rf value in paper chromatography, color reactions, paper electro-phoretic behaviors, and ultraviolet absorption. It was found that both substances were identical.
2. The wild strain and various eye-color mutant strains (including five recessive and six double recessive strains) were examined for the presence of xanthurenic acid. The wild, st, bw, se, and se st strains were positive for it, while the v, cn, v bw, cn, bw, bw st, v se, and cn se strains were negative. These results are discussed from the point of view of tryptophan metabolism.
The authors wish to express their gratitude to Professor Yahito Kotake of the Wakayama Medical College for the generous gift of synthetic xanthurenic acid, and to the Mizuno Laboratory, Faculty of Pharmacy, Kanazawa University, for the measurements of ultraviolet absorption. Thanks are also due to Dr. G. Tomita of the Tohoku University for his kindness in reviewing this manuscript.
This work was supported by a Grant in Aid for Miscellaneous Scientific Research from the Ministry of Education.View full abstractDownload PDF (430K) -
V. PURIFICATION OF IRPEX CELLULASE AND ITS ACTION UPON p-NITROPHENYL β-CELLOBIOSIDEKAZUTOSI NISIZAWA1955 Volume 42 Issue 6 Pages 825-835
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A crystalline substance having relatively high cellulase activity was obtained from the culture solution of Irpex lacteus by fractionation with acetone. The specific activity remained unchanged by recrystallization, suggesting that the crystal itself might be regarded as cellulase.
2. The crystalline preparation was found to split besides CMC also p-nitrophenyl β-cellobioside both at agluconic and holosidic bond, although the enzyme preparation was completely free of cellobiase.
3. The rate of the enzymic hydrolysis of the holosidic bond of p-nitrophenyl β-cellobioside fell rapidly with time. On the basis of inhibition experiments this phenomenon was interpreted in terms of a specific inhibition of cellulase by the split products such as glucose, cellobiose and β-glucoside. Phenol showed no inhibitory action upon the hydrolysis of this bond.
The writer wishes to express his deep gratitude to Dr. T. Miwa, Professor in the Tokyo University of Education, for his valuable discussion and advice, and to Dr. T. Kobayashi and Miss. N. Ichikawa for their technical assistance throughout this work.View full abstractDownload PDF (1118K) -
IV. FRACTIONATION OF THE ENZYME SYSTEM AND OCCURRENCE OF AN INTERMEDIATEYASUSHI WATANABE, SIMPACHI KONISHI, KENSUKE SHIMURA1955 Volume 42 Issue 6 Pages 837-844
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTwo enzymes which catalyse threonine synthesis from homoserine have been separated from Baker's yeast extract by ammonium sulfate fractionation. It has become apparent that two distinct reactions are involved in the over-all reaction. With Enzyme I, associated with the fraction precipitating at lower salt concentration, a stable precursor for threonine is synthesized from homoserine and ATP in the presence of Mg++, then the product acts as specific substrate for Enzyme II, which is associated with the fraction precipitating at higher concentration of the salt, resulting in the formation of threonine even in the absence of ATP.View full abstractDownload PDF (527K) -
KUNIO YAGI, YOSHITAKA MATSUOKA1955 Volume 42 Issue 6 Pages 845-847
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA circular paper chromatography was applied for the purification of FAD contained in the extract of Eremothecium ashbyii. By relatively simple procedures, FAD powder was obtained in an yield of 58.5 per cent and the purity was 43.3 per cent.View full abstractDownload PDF (193K) -
1955 Volume 42 Issue 6 Pages e1
Published: 1955
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (30K)
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