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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-
- Issue 1 Pages 1-
Volume 47, Issue 6
Displaying 1-19 of 19 articles from this issue
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KUNIHIKO SAITO1960 Volume 47 Issue 6 Pages 699-709
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. On trial analysis of a synthetic fatty acid mixture (using the material in three forms, the original non-treated, oxidized and hydrogenated), reversed-phase column chromatography is shown to be employed for the analysis of a fatty acids complex, provided that the material could be available in a quantity of 200 to 300mg.
2. Fatty acids obtained from B. alcaligenes faecalis, S. pullorum, B. fluorescens, S. typhi murium and B. Natto were analysed by this method.
3. Palmitic and unsaturated C18 acids were found to be the main com-ponents. Unsaturated C16 acids were also found to some extent. Among the unsaturated C16 and C18 acids the amount of palmitoleic and oleic acids seemed to be predominant.
4. A saturated C15 acid was found abundantly in the fat of B. Natto. The author wishes to thank Prof. S. Akashi, for the gift of the material and his interest during the present work.View full abstractDownload PDF (598K) -
STRUCTURE OF SUBTILOPENTADECANOIC AND SUBTILOHEPTADECANOIC ACIDSKUNIHIKO SAITO1960 Volume 47 Issue 6 Pages 710-719
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Subtilopentadecanic and subtiloheptadecanoic acids constitute a great proportion of the fatty acids obtained from B. subtilis, being roughly 50 and 15 per cent respectively.
2. The two acids were isolated by reversed-phase column chromatography and found to be C15 iso-and C17 iso-acids, v. z. 13-methyltetradecanoic and 15-methvlheaadecanoic acids.
The author wishes to thank Prof. S. Akashi, for the gift of the material and his interest in this work and to Dr. K. Nakanishi and Dr. Y. Iidaka for the measure-ment of infrared and X-ray diffraction, and to Prof. D. J. Hanahan, for his kindness in reading this manuscript.View full abstractDownload PDF (533K) -
VII. THE CONVERSION OF GLYCINE TO SERINE IN THE SILKWORM LARVATOSHIFUMI FUKUDA1960 Volume 47 Issue 6 Pages 720-725
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. To clarify the conversion of glycine to serine in the silkworm, glycine-l-C14 and glycine-2-C14 was given per os to the silkworms, and then serine was isolated from the fibroin and the sericin produced by these silkworms. The serine had a comparatively high radioactivity in its molecule.
2. The carbon of the carboxyl group and the carbon-2 atom of glycine are respectively used for synthesis of the carbon of the carboxylic group and the carbon-2 and -3 atom of serine in the silkworm.
3. It was found that glycine is converted to glyoxylic acid in the silk-worm by clarifing the existence of radioactivity in the glyoxylic acid which was isolated from the body fluid of the silkworms to which glycine-l-C14 was given per os.
4. These facts seem to suggest that serine which is contained in com-paratively high amount in fibroin (15 per cent) and in sericin (30 per cent) is derived not only directly from the serine in the mulberry leaves eaten by silkworm, but also from the serine which was synthesized from the glycine in the silkworm body.View full abstractDownload PDF (758K) -
TAKURO OGATA1960 Volume 47 Issue 6 Pages 726-732
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEmploying the central part of M. soleus of rabbits as a red muscle fiber preparation and the posterior edge of M. adductor magnus as a white muscle fiber preparation, the quantitative differences of some labile constituents and some enzymatic activities between the red and the white muscle fibers were estimated and the following results were obtained.
1. The histochemical study of succinic dehydrogenase demonstrated that the red muscle fiber preparatoin used practically free of white muscle fiber and vice versa.
2. The white muscle fibers contained about 3.7 times as much glycogen as the red muscle fibers.
3. The white muscle fibers contained about 2 times as much creatine phosphate and Δ7 phosphate as the red muscle fibers. Total acid-soluble phosphate was rich in white muscle fibers, while inorganic phosphate was rich in red muscle fibers.
4. The activity of oxidation of succinate and pyruvate was about 6 times higher in the red muscle fibers than in the white muscle fibers.
5. The activity of anaerobic glycolysis was about 1.7 times higher in the white muscle fibers than in the red muscle fibers.
6. The activity of adenosine triphosphatase was about 3.3 times higher in the white muscle fibers than in the red muscle fibers.
Author's acknowledgements are expressed to Prof. D. Jinnai for his kind advice and proof reading and to Prof. K. Ogata of the Department of Biochemistry of Niigata University Medical School for his valuable assistance in the course of the present, experiments.View full abstractDownload PDF (1184K) -
SABURO ISAKA1960 Volume 47 Issue 6 Pages 733-740
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Acidic ionization constants of some unsaturated amines were determined in 70 per cent dioxane solution. The order of pK values was as follows neocuproin>o-phenanthroline>bathocuproin>2, 9-diphenyl-4, 7-dimethyl-phen-anthroline (PMP)>bathophenanthroline>dipyridyl>diquinolyl.
2. The acceleratory effect of cupric ions upon the oxidation of DOPA was activated when some unsaturated amines were added. When the mixing ratio of copper to amines was 1:1, the order of the activity coincided with that of their pK values. Beyond this ratio, some of them decreased more or less in activity while some enhanced further the catalytic activity of the cupric ions.
3. The catalytic power of cupric ions upon the oxidation of urate was. also activated if some amines were added. The order of the activity was as follows: 1) o-phenanthroline>bathophenanthroline, 2) neocuproin>batho-cuproin>PMP, 3) dipyridyl>diquinolyl. These orders in each group coincide with those of their pK values. Discussions were made concerning the catalytic activity of the amines referring to their steric configurations.
The author is greatly indebted to Prof. Adrien AIbert of the Australian National University who has read the manuscript and made valuable comments on it.View full abstractDownload PDF (502K) -
I. ENZYMATIC FORMATION OF XYLULOSE IN RAT LIVERKEIKO FUKUNAGA1960 Volume 47 Issue 6 Pages 741-754
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Xu was identified to be the reaction product from either DHF, HPA or TAS, and Gla by purified rat liver transketolase.
2. The amounts of Xu formed from HPA was less than that from DHF, which requires two steps of decarboxylation to give “active glycolaldehyde”, Possible explanation for this was discussed.
3. DHF was found to be decarboxylated enzymatically. The decarboxyl-ase was purified 13-fold from acetone powder of rat liver. It required divalent cations such as Mn++, Co++ for activation. pH optimum was pH 5.0. This enzyme was distinct from oxaloacetic acid decarboxylating enzymes and exhibited no activity with OAA at pH 5.0.
4. The main product of decarboxylation was identified to be TAS.
The author wishes to express her gratitude to Dr. K. Kuratomi for his kind guidance and encouragement throughout the investigation and to Prof. T. Sekine and Prof. S. Akabori for their continuous interest.
This work was supported in part by a grant for scientific research from the Ministry of Education.View full abstractDownload PDF (764K) -
ICHIRO HARUNA1960 Volume 47 Issue 6 Pages 755-763
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A new protein, named H-albumin, was obtained in crystalline form from native ovalbumin incubated with a bacterial proteinase BPN' accom-panied with the liberation of three peptides in trichloracetic acid soluble form.
2. The composition of amino acids of the whole peptides is Glu1, Asp2, Gly2, Ser2, Ala4, Thr1, Phe1, Val3, (Leu or Ileu)3, Lys1.
3. The new protein was suggested to have one N-terminal (Thr) and two C-termineals (Val and Pro).
The author's thank is due to Dr. Jirgensons who kindly supplied with DFP-treated carboxypeptidase and to Prof. Akabori, by whose continuous encouragement the present work has been conducted.View full abstractDownload PDF (556K) -
LEO M. SREEBNY, BARBARA WANAMAKER, DONALD BECHLEM1960 Volume 47 Issue 6 Pages 764-770
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (376K) -
YOSHIO UENO, HIROSHI OYA, TAKEO BANDO1960 Volume 47 Issue 6 Pages 771-776
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A method of column chromatography was described, in which 0.2 N H2SO4 on Celite was used as the stationary phase and n-butanol-chloroform or isoamyl alcohol-chloroform mixtures as the solvent system.
2. Main intermediates of the tricarboxylic acid-cycle were separated by the above mentioned two solvent systems and determined by titration with 0.002 N KOH. The recovery of the acids ranged from 80 to 90 per cent.
3. This method was applied to the determination of the amount of members of the tricarboxylic acid-cycle in tissues of normal rat. The results were in good accord with the previous reports obtained by different procedures.
4. Application of the above mentioned method to the tissues of Ascaris lumbricoides var. suis showed that succinic acid was the main component in muscle as well as perienteric fluid, whereas no significant amount of tri-carboxylic acids were discovered in these tissues. Problems concerning metabolism in ascaris were discussed from this unique feature in distribution of the acids found.
The authors wish to express their thanks to Prof. Y. Kobayashi and to Dr. S. Ebashi for their continued interest in this work, and to Dr. T. Tatsuno for synthe-sizing a-ketoglutaric and oxalacetic acids. The authors were also indebted to Miss K. Hamano for her technical assistance.View full abstractDownload PDF (326K) -
I. DETERMINATION OF LIPOPROTEIN LIPASEMASAYA SUEHIRO, KAZUO NAKANISHI1960 Volume 47 Issue 6 Pages 777-780
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA modified method for the quantitative assay of lipoprotein lipase based on the determination of glycerol has been presented. After the deproteiniza-tion of enzymatic reaction mixture with trichloroacetic acid, the filtrate obtained was oxidized with periodate and the resulting formaldehyde was coloured with chromotropic acid without disturbance.View full abstractDownload PDF (193K) -
V. N. BUKIN, G. V. PRONYAKOVA1960 Volume 47 Issue 6 Pages 781-786
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (360K) -
III. STIMULATORY ACTION OF GLUCOSE ON INDUCED FORMATION OF HISTIDINE DECARBOXYLASESOHACHI ANDO1960 Volume 47 Issue 6 Pages 787-793
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSWhen washed cells of Proteus morganii was incubated in induction media containing glucose, fructose, ribose, galactose, gluconate, or pyruvate, re-spectively, for carbon source, induced formation of histidine decarboxylase was performed at the same rate in respective media, while the rates of the growth of cells in induction media differed from each other.
Washed cells also formed inducibly the enzyme in an induction medium containing casamino acid for carbon and nitrogen sources. By the addition of certain compounds, such as glucose, ribose, gluconate, or pyruvate, to casamino acid medium the induction of the enzyme was stimulated markedly. The possible mechanism of the stimulatory action of these compounds were discussed.
The author wishes to thank Prof. S. Akabori and Prof. K. Miyaki for their interest and encouragement, and Prof. T. Sasakawa and Dr. M. Hayashi for their valuable advice and discussion.View full abstractDownload PDF (421K) -
II. THE REACTION MECHANISMS OF TURNIP PEROXIDASES A1, A2 AND DTOICHIRO HOSOYA1960 Volume 47 Issue 6 Pages 794-803
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The kinetics of the over-all reaction of the purified turnip peroxidases A1, A2 and D has been studied using guaiacol and ascorbic acid as the hydrogen donor.
2. The reaction mechanisms of these enzymes were found to be essenti-ally of the same nature as each other and as that of horseradish peroxidase, but the relationship between the reciprocal of the rate of over-all reaction and the reciprocals of the concentrations of hydrogen peroxide and hydrogen donor was different from that for horseradish peroxidase, only in that there is an additional absolute term (independent of the concentrations of hydrogen peroxide and hydrogen donor) in the case of the enzymes here studied.
3. This term was interpreted by two probable mechanisms, and the values of the rate constant of each reaction step were computed and compared with that of horseradish peroxidase.
The author wishes to express his thanks to Profs. B. Tamamushi, and S. Nagakura of the University of Tokyo, and Prof. N. Ui of Gunma University for their invaluable advice and encouragement. His thanks are also due to Prof. Y. Ogura of the University of Tokyo, not only for his criticism, but also for his interest and encouragement. This study was aided in part by a Grant-in-Aid for Scientific Research from the Ministry of Education given to the Research Group on “Mechanism of Enzyme Action”.View full abstractDownload PDF (538K) -
AKIO MAEDA, ATSUSHI OIKAWA, SHIRO AKABORI1960 Volume 47 Issue 6 Pages 804-808
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Native, dialyzed and urea-denatured taka-amylase A (TAA) were compared each other in their temperature-dependence of optical rotatory power. Urea-denatured TAA shows a negative temperature coefficient of this power. Native TAA also shows the same phenomenon above 30°, though lesser extent, and below this temperature, the rotatory power remains constant.
2. TAA has two different values of energy of activation for its catalytic action to a substrate, α-phenylmaltoside. The critical temperature of this difference is about 37°.
3. The rate of amino acid liberation from TAA also shows a distinct change at this temperature.
4. These facts were discussed in reference to the structure of this enzyme.View full abstractDownload PDF (274K) -
NOBU AKAMATSU, JR.1960 Volume 47 Issue 6 Pages 809-819
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSpecificity of the hydrolytic enzymes for several hydantoin compounds, dihydropyrimidines and ureido acids was investigated in view of their adaptive formation in soil bacteria.
The enzymes for the reversible opening of hydantoin rings are of adaptive nature and their specificity is determined by the length of side chains of the substrates. Hydantoin acetic acid and hydantoin propionic acid are hydrolyzed by enzymes different from each other.
So far as studied with dihydrouraeil, dihydroorotie acid, 5-hydroxy-dihydrouracil and dihydrothymine, those dihydropyrimidines are decomposed to corresponding carbamyl amino acids by an enzyme system of constitutive nature.
The decarbamylating enzymes for ureido acids are produced by adapta-tion and their substrate specificity for ureido acids depends upon the difference of amino acid moiety. Hydrolysis of carbamyl aspartic acid and carbamyl glutamic acid is carried out by ureidosuccinase and ureidoglutarase, respective-ly. However, carbamyl β-alanine, carbamyl isoserine and β-ureidoisobutyric acid are hydrolyzed by a single enzyme. Therefore, substitution at α-carbon of β-alanine moiety, may it be by hydroxyl or methyl group, does not effect the specific combination of the enzyme with the β-ureido acid of C3 chain length. The, soil bacteria grown on media containing uracil as a sole nitrogen source produced ammonia from isobarbituric acid, but not from barbituric acid. A possible hydration of uracil as one of metabolic pathways was discussed.
Expenses of this work were defrayed by Grants for the Advancement of Science delivered by the Department of Education, Japan, to Prof. S. Akamatsu.View full abstractDownload PDF (690K) -
I. ENZYMATIC OXIDATION OF α-NAPHTHYLAMINE IN RICE PLANT ROOTSHOOICHI MATSUNAKA1960 Volume 47 Issue 6 Pages 820-829
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The partially purified peroxidase from leaf and root of rice plant respectively and crystalline peroxidase named JRP-a from Japanese raddish can oxidize α-NA with H2O2. The oxidized product of α-NA was a dark violet colored substance, and was soluble scarcely in water, slightly in ethyl ether and very easily in ethylacetate. β-NA was also oxidized by this enzyme system as well as α-NA.
2. The peroxidatic oxidation of α-NA needs one mole of H2O2 per one mole of α-NA.
3. The α-NA-oxidizing activity which seems to be available for the method of diagnosing of the root activity in agronomy, may represent the rate of the production and supply of H2O2 or other peroxides in tissue to be measured.
I wish to express my thanks to Dr. Y. Morita for supplying the crystalline pero-xidase used in this study, and also to Dr. I. Yamazaki for his helpful suggestions.View full abstractDownload PDF (523K) -
I. PURIFICATION AND PROPERTIES OF TAKA-MALTASE FROM TAKA-DIASTASETAIJIRO MATSUSHIMA1960 Volume 47 Issue 6 Pages 830-836
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTwo maltases (α-glucosidases), Taka-maltase I and II, were separated from taka-diastase, by means of column chromatography using weak anion exchange resin, Duolite A-2. Their properties were determined and discussed.
The author wishes to express his deep gratitude to Prof. S. Akabori for his kind guidance and to Dr. T. Ikenaka for his valuable advice throughout the investigation, and also to Sankyo Co., Ltd. for their kind supply of ‘Takadiastase Sankyo.’View full abstractDownload PDF (384K) -
III. NATURE OF TERMINAL ELECTRON TRANSPORT SYSTEM AND ITS SENSITIVITY TO CYANIDESHÔJI MIZUSHIMA, KEI ARIMA1960 Volume 47 Issue 6 Pages 837-845
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Water soluble preparation which catalyzes the electron transfer between DPNH or succinate and oxygen was obtained from subcellular particulate preparation of a strain of Achromobacter.
2. Cytochrome b1 and a2 contained in the preparation were slowly reduced by succinate or DPNH and oxidized in an instant by oxygen.
3. Cyanide (10-3M) remarkably but not completely inhibited the oxido-reduction of cytochrome a2 but did not inhibit the reduction of cytochrome b1.
4. The direction of electron transport between succinate or DPNH and oxygen was postulated as follows;
5. These results supported a view on the mechanism of cyanide resistance in this bacteria.
The authors wish to express their sincere appreciation to Dr. K. Sakaguchi for his encouragement and advice in this investigation, and are indebted to Dr. K. Okunuki Osaka University for his kind suggestion and discussion.View full abstractDownload PDF (527K) -
KANTARO SUZUKI, YOSHITAKE MANO, NORIO SHIMAZONO1960 Volume 47 Issue 6 Pages 846-849
Published: June 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (214K)
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