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Volume 37 (1950)
- Issue 4 Pages 381-
- Issue 3 Pages 289-
- Issue 2 Pages 145-
- Issue 1 Pages 1-
Volume 37, Issue 2
Displaying 1-10 of 10 articles from this issue
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XIII. THE FATE OF DL-α-N-METHYLHISTIDINE IN THE ANIMAL BODY AND ITS ENZYMATIC DECOMPOSITIONJITSUWO UTSUNOMIYA1950 Volume 37 Issue 2 Pages 145-151
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A small amount of imidazolepyruvic acid was isolated from the urine of a dog injected subcutaneously with DL-α-N-methyl-histidine, but no urocanic acid. It was previously confirmed that the dog was able to transform L-histidine into urocanic acid.
2. Both dogs which were investigated, were able to put out urocanic acid after the subcutaneous injection of L-histidine. 3 rabbits, however, did not do so under the, same conditions.
3. Liver extract of rabbits and guinea pigs can desaminate L-histidine into urocanic acid, but not DL-α-N-methylhistidine.
4. DL-α-N-methylhistidine was reacted, at first with extract of rabbits kidney (demethylase), and subsequently that of rabbits liver (histidase), a small amount of urocanic and, imidazolepyruvic acids together with unchanged DL-α-N-methylhistidine was isolated.
This work was carried out by the aid of “Research Fund of Science” of the Department of Education, R. Hirohata.View full abstractDownload PDF (364K) -
Y. OGURA, Y. TONOMURA, S. HINO, H. TAMIYA1950 Volume 37 Issue 2 Pages 153-177
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) The reaction between catalase molecule and various inhibitory substances was studied quantitatively by using both kinetic and spectrophotometric methods.
2) The characteristic spectrum of catalase is changed by its combination with cyanide, chloride, fluoride, sulfide, azide and hydroxylamine, while no change could be observed by that with phenol, resorcinol, hydroquinone, cresols, chlorophenols, nitrophenols and hydrogen ion, though these strongly inhibit catalase activity. Substances of the latter group may be regarded as exerting their inhibitory action by combining with certain structual element in protein moiety of the catalase molecule.
3) In the absence of inhibitors, the Iog[H2O2]-time-curve observed in the catalatic H2O2-decomposition represents, as is well known, a straight line at lower temperatures and within certain limits of H2O2 concentration applied. In the presence of inhibitors, however, the log[H2O2)-time-curve usually bends more or less convexly towards the time-axis. The exception was found only in cyanide in which the log[H2O2]-time -curve represented a straight line as in the control experiment. The bending curves were found to be composed of two straight lines with different tangents, and for the corresponding two states of inhibition, referred to as the which is in accordance with the fact that in the absence of inhibitors the log[H2O2]-time-curve represents a straight line.
In the presence of an inhibitor the following two reaction will occur besides the above-mentioned three:
E+G_??_EG (IV)
SE+G_??_SEG (V)
Assuming that both these reactions can take place rather slowly, it was deduced that the φ-values found in the “initial” and “final” S states are the dissociation constants of EG and SEG, respectively, the former having larger dissociation constant than the latter. Among all the inhibitors studied, cyanide occupies a special position, in which reactions (IV) and (V) seem to occur very rapidly with the dissociation constants not differing from one another.
This investigation forms a part of the study of the Research Commitee of Heavy Metal Catalysis of the National Research Council and was supported by a grant donated to one of the authors (Tamiya) by the Ministry of Education.View full abstractDownload PDF (1278K) -
Y. OGURA, Y. TONOMURA, S. HINO, H. TAMIYA1950 Volume 37 Issue 2 Pages 179-204
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) Interactions between two poisons in their action upon catalase were studied both by kinetic and spectrophotom;tric methods. Based on the results obtained, poisons of catalase were divided into four types, i.e. Cyanide, Azide, Phenol and Hydrogen Ion Types. To each of these groups belong the following substances:
Cyanide Type: cyanide, chloride, fluoride and sulfide.
Azide Type: azide and hydroxylamine. Phenol Type: phenol, resorcinol, hydroquinone, cresols, chloro-phenols and nitrophenols.
Hydrogen Ion Type, of which hydrogen ion represents the only member thus far found.
The study of the mutual action of the substances belonging to the first mentioned three groups formed the subject of the present report.
2) Poisons belonging to the same group “compete” with each other for a definite active center of the catalase molecule; accord-ingly, two poisons, G1 apd G2, belonging to the same group cannot share one catalase molecule (E) at the same time. This was shown, not only by kinetic method but also spectrophotometrically-in the case of-substances of Cyanide and Azide Types-by the fact that on adding G1 and G2 in sufficient quantities, catalase solution shows only the mixed spectra of EG1 and EG2, the ratio of which depends upon the relative concentrations of G1 and G2 and their relative affinities toward E.
3) Poisons belonging to different groups are linked to different active centers in the catalase molecule, a conclusion which has partly been drawn in cur previous paper in which we inferred that the poisons of Phenol Type attach to the protein moiety, while those of Cyanide and Azide Types combine with protohemins of the catalase' molecule. Owing to the difference of the site of attachment, poisons belonging to different groups may be expected to link to one catalase molecule at the same time, forming a triple complex of the type EG1G2. This expectation was borne out not only by various kinetic experiments, but also-for the substances of Cyanide and Azide Types-spectrophotometrically by the discovery of a characteristic spectrum of EG1G2 which was essentially different from either that of EG1 or of EG2.
4) By analyses of various quantitative data, it was shown that the affinity of G1 to EG2 is not always the same as that between G1 and E; in other words, poisons belonging to different types can exert certain mutual influences in their combination with catalase molecule. The substances of the three categories dealt with in this paper were found to act upon each other more or less “repulsively”, i.e. G1 requires more energy to combine with EG2 than to combine with E. The data to be reported later will show that the hydrogen ion, when attached to catalase molecule, act “attractively” on phenols, but quite “indifferently” upon substances belonging to the Cyanide and Azide Types.
5) On the available data it may be concluded that the catalase molecule has at least four active or sensitive centers, each having affinities to the poisons or respective types mentioned above.
This investigation forms a part of study of the Research Commitee of Heavy Metal Catalysis of the National Research Council and was supported by a grant donated to one of the authers (Tamiya) by the Ministry of Education.View full abstractDownload PDF (1271K) -
I. SULFA COMPOUNDSYOSHIAKI MIURA1950 Volume 37 Issue 2 Pages 205-217
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (470K) -
K. SHIMAO1950 Volume 37 Issue 2 Pages 219-229
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (575K) -
SHOYO SAKAGUCHI1950 Volume 37 Issue 2 Pages 231-236
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A new colorimetric method for the determination of arginine based on a colour reaction with oxine and sodium hypobromite is reported.
2. A simple method of hydrolysis of protein for the arginine determination is reported.
In conclusion I wish to express my hearty thanks to Emer. prof. S. Kakiuchi and Prof. K. Kodama for their kind advice.View full abstractDownload PDF (315K) -
YUKI ITO1950 Volume 37 Issue 2 Pages 237-247
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) The maceration of Pen. notatum hydrolyzes protamine besides gelatin and peptone as proteins. It contains also dipeptidase (glycylglycine), tripeptidase (triglycine, leucyldiglycine), hippurase, carboxydipeptidase, acylase (acetylglycine, acetylglutamic acid) and halogenacylase (Cl-acetylleucine, Cl-acetylphenylalanine).
2) Both maceration and acetone powder are able to attack diglycine and-benzoylglycine. The hippurase has rather resistance against acetone treatment contrary to the dipeptidase. The optimum pH for the hydrolysis of glycylglycine is found to be at pH 7.5, that for benzoylglycine at pH 7.0 and that for benzoyldiglycine near at pH 6.0. Benzoic acid was isolated as the product of hippurase action.
3) Moldenzymes are unstable against acid, leaving only peptone (Riedel)- and benzoylglycine-splitting activity by keeping at pH 4.0 and 37° for 5 to 60 minutes, but these actions diminish after incubation for 90 to 120 minutes.
4) They are rather resistant to alkali and show no inactivation when kept at pH 9.0 and 37° 17 hrs. When the maceration is kept at pH 11.5 and 37°C, it loses activity of gelatin- as well as benzoyldiglycine-splitting after incubation for 60 minutes and it remains only action of peptone (Riedel)- and slight benzoylglycine-splitting after treatment for 120 minutes. Peptonase and hippurase are more resistant against both treatments than others.
In closing the author wishes to express his deepest gratitude to Dr. S. Utzino, Prof. at the Department of Medicine, Kyoto University, for his kind constant guidance in this research. The author is also indebted to Prof. Nakamura (Osaka University) for preparing the Penicillium mycelium.
These investigations owed much to the aid-grants given by the Ministry of Education for the Scientific Researches, for which author's thanks are here expressed.View full abstractDownload PDF (580K) -
Y. OGURA, Y. TONOMURA, S. HINO1950 Volume 37 Issue 2 Pages 249-267
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS(1) In, continuation of works previously reported, quantitative studies were made on the transition phenomena occuring in the inhibitory action of various poisons upon catalase reaction. Further evidence was adduced in support of the hypothesis, advanced in the preceding paper, that the “fina” state of inhibition is brought about by the reaction of the poison with the catalase-H2O2-complex which is formed in an intermediate step of the catalase reaction.
(2) Using azide and o-chlorophenol, the velocity constant of the reaction between the catalase-H2O2-complex in question and the -poisons was determined. From the data on the effect of ionic -strength of the medium upon the velocity of the said reaction, it was concluded that the reaction between the complex in question and azide is non-ionic, while the reaction between the complex and, -o-chlorophenol is ionic.
(3) By the pretreatment-technique, as was effected with H2O2 in our previous work, it was shown that a compound quite homolo-gous to the catalase-H2O2-complex mentioned above is formed bet-ween catalase and monomethyl hydrogen peroxide. This compound was found to combine with various poisons with the affinities which are of the same order of magnitude as those shown by the catalase-H2O2-complex towards the respective poisons.
(4) It was discussed that the cat alase-H2O2-complex, the formation of which was studied kinetically by Chance using the technique of flow-method, is nothing but the complex postulated in the authors' theory. Taking duly into account the data reported by Chance (8) and by Bonnichsen, Chance and Theorell (9) and also by using some data obtained in the authors' experiment to be reported later, concrete values of velocity constants were assigned to each intermediate step of catalase reaction assumed in the authors' theory. It was thus shown that the kinetic schema:
E+S_??_SE
SE+S_??_SSE
SSE→E+2H2O+O2
(E: free catalase molecule, S: hydrogen peroxide, SE: the intermediate complex, SSE: a complex in which another molecule of H2O2 s is bound reversibly to SE), represents the simplest and satisfactory picture in alignment with all kinetic evidences known for the process of H2O2 decomposition by catalase.
The authors desire, in this opportunity, to thank Dr. H. TAMIYA for his -encouragement and support in carrying out this research. Thanks are also due to the Ministry of Education for a grant which enabled the research to be carried out.View full abstractDownload PDF (958K) -
SADAO OKAMOTO1950 Volume 37 Issue 2 Pages 269-274
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Diastase values in the organs and tissues of rabbits, rats, guinea pigs, bull frogs, frogs, chicken and pigeons were determined by the method of Nakahira. Also, glycogen quantities in the organs and tissues were determined by Yamamoto's method at the same time.
2. Among animals, rats and guinea pigs indicated highest diastase values in their organs and tissues.
3. Diastase values were higher in the order of kidneys, livers and lungs in various organs and tissues, while, lower in skins, muscles and brains.
4. In chicken, no demonstrable amylolytic enzyme was found in skins and brains.
5. It appeared that very little relation existed between the diastase value and glycogen of respective organs and tissues.View full abstractDownload PDF (298K) -
TÔRU ISHII1950 Volume 37 Issue 2 Pages 275-287
Published: 1950
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) In spite of the remarkable increase of blood sugar in the alloxan-diabetic rabbits, their lactate., pyruvate and the ratio of lactate to pyruvate in the blood were of the same levels as in the normal rabbits.
2) When insulin was injected, a distinct decrease of the blood pyruvate and lactate was observed during the hypoglycemic state in the normal rabbits, whereas a temporary decrease and a following increase of the blood pyruvate and lactate were observed in the alloxan-diabetic rabbits.
3) When glucose was injected, the blood pyruvate and lactate as well as glucose were increased in the normal rabbits, but no increases of the former two were observed in the alloxan-diabetic rabbits.
4) When insulin was injected with glucose, blood lactate and pyruvate showed a distinct increase in both normal and diabetic rabbits, although the course was somewhat different between them.
5) The rate of disappearance of the injected pyruvate from the circulating blood showed no remarkable differences between normal and diabetic rabbits.
6) In the hypoglycemic phase of alloxan injection the blood lac-tate and pyruvate were never decreased, or in some cases some-what increased.
This work was supported by a grant from the Department of Education for scientific research. The author gratefully acknowledge the guidance and helpful advices of Prof. N. Shimazono.View full abstractDownload PDF (708K)
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