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Volume 48 (1960)
- Issue 6 Pages 781-
- Issue 5 Pages 623-
- Issue 4 Pages 469-
- Issue 3 Pages 317-
- Issue 2 Pages 161-
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Volume 48, Issue 3
Displaying 1-18 of 18 articles from this issue
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IV. PROPERTIES OF CHROMOPEPTIDES DERIVED FROM PHYCOERYTHRIN BY THE ENZYMIC DIGESTIONTERUKO FUJIWARA1960 Volume 48 Issue 3 Pages 317-330
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Various chromopeptides soluble in organic solvents, were obtained from the peptic, tryptic, B. subtilis N' and S. griseus proteolytic digests of phycoerythrin of Porphyra tenera.
2. Absorption maxima of these chromopeptides were from 490 to 600μg.
3. The core chromopeptides of phycoerythrin containing Asp, Glu, Ser, Gly, Ala, Val, Leu and Ileu could be obtained by the proteolysis.
4. Most of the chromopeptides had a low nitrogen content (5-6 per cent) and about 0.6 to 1.5 per cent of sulfur.
5. The sugar contents of the chromopeptides, P-11a, -llb and -12a were 13.01, 7.79 and 3.89 per cent (glucose values) respectively. Galactose, arabinose and xylose were found in P-12a.
The author wishes to express her sincere gratitude to Prof. S. Akabori for his constant interest and encouragement throughout this investigation. She also wishes to thank Prof. K. Okunuki and Dr. H. Matsubara, Faculty of Science, Osaka University for supplying crystalline Bacillus subutilis proteinase, and Miss. T. Kawano, Osaka College of Pharmacy for bioassay.View full abstractDownload PDF (1475K) -
IV. ON THE NATURE OF GLUCOSAMINE OXIDATION BY PSEUDOMONAS FLUORESCENSYUJIRO IMANAGA1960 Volume 48 Issue 3 Pages 331-340
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The glucosamine oxidizing activity in crude extract of Pseudomonas fluorescens was found to be localized in some particulate matter.
2. The particulates oxidized only glucosamine and glucose and had almost no activity toward several other sugars including galactosamine.
3. In these particulates, a dehydrogenase which might be called glucosamine dehydrogenase participated in the glucosamine oxidation through some cytochrome system.
4. The glucosamine dehydrogenating enzyme was extracted into high speed supernatants (about 100, 000×g) by digitonin treatment.View full abstractDownload PDF (476K) -
YOSHIO IMAI, SUZUOKI ZIRO, AKIRA KOBATA1960 Volume 48 Issue 3 Pages 341-350
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. In the present study on the fate of S35-labeled 4-methyl-5-β-hydroxy-ethylthiazole (Th) in rats, 85-95 per cent of the radioactivity administered intraperitoneally or intravenously was excreted into urine within 24 hours and there was found no accumulation of the radioactivity at any organ investigated.
2. The radioactive urinary metabolites were investigated by ion exchange chromatography, paper chromatography and paper electrophoresis. Urinary excretion pattern of Th-S35 in the case of a small dose (1mg. per rat) was the same as in a large dose (100mg. per rat). The majority (about 95 per cent) of the metabolites was isolated, characterized and identified with 4-methylthiazole-5-acetic acid. Several radioactive components including unchanged Th were also demonstrated, although each amounts to only one per cent or less.
The authors are deeply iedebted to Mr. T. Iida for his technical assistance, to Dr. Kanzawa and Mr. Nishikawa for the infrared spectroscopy and to Dr. Tanabe, Mrs. Kan, Kashiwagi, Suzuki and Tsukamoto for elementary analysis and to Dr. Hirano and Mr. Tsujikawa for the synthesis of ThA.View full abstractDownload PDF (1343K) -
I. ENZYMATIC ACTION OF LYSOZYME ON GLYCOL CHITINKOZO HAMAGUCHI, KAZUKO ROKKAKU, MASARU FUNATSU, KATSUYA HAYASHI1960 Volume 48 Issue 3 Pages 351-357
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSUsing glycol chitin as substrate, several enzymatic properties of egg white lysozyme were examined. The results were as follows.
1. A rapid decrease in viscosity and increase in reducing power and intensity of color produced by the Elson-Morgan reaction were observed on hydrolysis of glycol chitin by lysozyme.
2. The optimum pH and temperature for lysozyme activity were found to be at pH 3.5 and 50°, respectively. Lysozyme was unstable at pH's below 2.5 and above 10.0.
3. The stability of lysozyme decreased in solution of urea more concentrated than 4M.
4. Pretreatment of lysozyme by heat increased its activity. Heat inactivation was not observed at temperature below 80°. However, in boiling water lysozyme was inactivated.
5. Glycol chitosan was not hydrolyzed by lysozyme.
The authors wish to express their hearty thanks to Prof. T. Isemura for his kinds support, and to Dr. R. Senzyu of Kyushu University who supplied glycol chitin and glycol chitosan, and to Dr. Y. Imanaga of Nara Women's University who supplied glucosamine hydrochloride.View full abstractDownload PDF (366K) -
II. EFFECT OF UREA ON LYSOZYMEKOZO HAMAGUCHI, KAZUKO ROKKAKU1960 Volume 48 Issue 3 Pages 358-362
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTo study the relationship between changes in activity and the physico-chemical properties of lysozyme, we measured the intrinsic viscosity and optical rotatory dispersion constants at various concentrations of urea.
The intrinsic viscosity of lysozyme in 8M urea was the same as that of native lysozyme at 33.0°. The dispersion constant of lysozyme in 8M urea was only slightly smaller than that of the native protein.
The inactivation of lysozyme by urea was not in parallel with the change in the viscosity and the dispersion constant at 33°. However, the inactivation and the change in reduced viscosity of lysozyme at higher temperatures were in parallel. It was suggested that a change in fine structure of the lysozyme, which was not reflected by changes in the intrinsic viscosity or dispersion constants, was responsible for its inactivation.
The authors wish to express their hearty thanks to Prof. T. Isemura of the Institute and to Prof. M. Funatsu and Dr. K. Hayashi of the Kyushu University for their encouragements in the present experiments.View full abstractDownload PDF (287K) -
AKIO MAEDA1960 Volume 48 Issue 3 Pages 363-374
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A method of preparation of RNA from yeast 80S particle which gives high yield and consistently high molecular weight was described. The pH and temperature are especially important.
2. RNA prepared in such a manner has the value of 28S along with 19S in sedimentation constant, 0.55 dl./g. in intrinsic viscosity and 0.82×10-7 cm.2/sec. in diffusion constant.
3. RNA dissociates irreversibly into small sub-units (about 5S) above 40° or in the presence of EDTA in low temperature. The significant change in optical density occured around 40°.
4. RNA prepared by phenol method still contains ribonuclease and liberated acid soluble nucleotides especially in the presence of EDTA.
5. From the viscosity behavior and the specific rotation of 190° at 589, mμ, configurational properties of RNA was discussed.
Author wishes to express his thanks to Prof. F. Egami for his interest and encou-ragement through this work and to Dr. S. Osawa and Dr. K. Takata of the Department of Biology, Dr. S. Asakura of the Department of Physics and Dr. T. Takagi of the Division of Physical Chemistry, Institute for Protein Research, Osaka University, for their fruitful discussions and making facillities for earring out measurements.
Thanks are also due to the Institute for Protein Research, Osaka University, for the use of Cary spectrophotometer and Mr. S. Tsukamoto, the Department of Micro bioloby, Medical School of Nagoya University, for the operation of Spinco model E. Author is much indebted to Prof. T. Isemura, the Institute for Protein Research, Osaka University, for permitting a part of this study in his laboratory. The expense of this study was defrayed in part by grant from the Ministry of Education.View full abstractDownload PDF (2287K) -
V. THE EFFECT OF SEVERAL CHEMICAL REAGENTS UPON THE ACTIVITY OF TURNIP PEROXIDASE DTOICHIRO HOSOYA1960 Volume 48 Issue 3 Pages 375-381
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. When turnip peroxidase D was treated with acetic anhydride, nitrous acid, and 2, 4-dinitrobenzene sulfonic acid, the activity of the enzyme was found to decrease remarkably, rather owing to the decrease of the rate of reaction of Complex II with hydrogen donor. This finding seems to support the view set forth previously from kinetic studies that a certain amino group of the protein moiety of the enzyme may play an essential role in the reaction of Complex II with hydrogen donor. The rate of the formation of Complex I, however, also decreased more or less, especially in the case of the treatment with 2, 4-dinitrobenzene sulfonic acid. A possible cause of the decrease was discussed.
2. The absence of free sulfhydryl group in the protein moiety of the enzyme was confirmed by kinetic and spectrophotometric studies.
3. Diazobenzene sulfonic acid did not cause any loss of the activity of the enzyme. Iodine showed a slight inhibitory effect, which seemed, however, to be due to the denaturation of the enzyme caused by the reagent. From these results, it may be inferred that imidazole and phenolic groups of the protein moiety are not essential for the activity of the enzyme.
The author is indebted to Prof. N. Ui of Gunma University and Prof. Y. Ogura, of the University of Tokyo for their invaluable advice and encouragement. This study has been supported 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 (381K) -
II. FURTHER EVIDENCES FOR BROAD SPECIFICITY OF THE AMYLASETERUO SAWAI1960 Volume 48 Issue 3 Pages 382-391
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe action of amylase preparations of Candida tropicalis var. japonica was shown to extend to the hydrolysis of isomaltose and α- and β-amylase limit dextrins, with the same optimal pH (4.0) as previously found for hydrolysis of soluble starch, maltose and hetero α-glucosides, and for transglucosylation from α-phenyl glucoside to glycerol. Starch block electrophoresis of several enzyme preparations, using buffers of widely separated pH (7.0 and 2.8), showed that all of the above activities had the same electrophoretic distribution, strongly suggesting that a single enzyme mediates all activities.
Additional evidence on the same point was obtained through studies involving the inhibitory action of various carbohydrates on starch hydrolysis by Candida amylase preparations. Thus, a remarkable parallelism was found between the capacity of certain carbohydrates to suppress the utilization of soluble starch and their capacity to suppress the splitting of α-phenyl glucoside. Maltose, in particular, was found to be an extremely potent inhibitor of both activities. Moreover, the Michaelis constants for maltose, α-methyl glucoside and α-phenyl glucoside were found to be of the same order, respectively, as the dissociation constants obtained when these substrates were used to inhibit the hydrolysis of soluble starch. Finally, the inhibition of starch hydrolysis by these three compounds, as in the case of glucose, proved to be competitive.
The author wishes to express his thanks to Prof. T. Miwa and to Prof. T. Mori for their valuable suggestions and encouragement; to Dr. K. Shibasaki for a supply of isomaltose and to Dr. N. Suzuki for making available the apparatus for electrophoresis. Prof. Edward J. Hehre of the Albert Einstein College of Medicine, New York, helped prepare the manuscript for which the author is very grateful.View full abstractDownload PDF (632K) -
TOSHIO MISHIMA, YOSHIMI OKADA, TAKEO TERAI, KATSUHIKO OGURA, YUICHI YA ...1960 Volume 48 Issue 3 Pages 392-396
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSLipide component of proteolipide was fractionated by silica gel chromatography and cord factor was isolated in a good yield.
This work was supported in part by grants of Ministry of Education and Ministry of Welfare and Health.View full abstractDownload PDF (297K) -
IV. ON THE C-TERMINAL REGION OF BACTERIAL AMYLASEKIN-ICHI SUGAE1960 Volume 48 Issue 3 Pages 397-405
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe C-terminal amino acid of BA (B. subtilus N') was analyzed by hydrazinolysis and by the use of carboxypeptidase. From the results of hydrazinolysis, it was suggested that C-terminus of BA might be glycine. While, a considerable amount of amino acid was released by the action of carboxypeptidase on native bacterial amylase and no decrease of the amylase activity was observed. Amino acids liberated by carboxypeptidase are leucine and/or isoleucine, valine, phenylalanine, alanine, acidic amino acids, tyrosine, threonine, serine, asparagine and glycine.
In contrast to the case of hydrazinolysis, it is remarkable that leucine, valine and phenylalanine are liberated in much larger amounts as compared to that of glycine. No clear cut result was obtained about the nature of C-terminal group of BA. However, it might be suggested that C-terminus of BA is not essential for the enzymatic activity.
The author wishes to thank Prof. S. Akabori for his helpful advice throughout this work and also to Nagase Ltd. Co. for the gift of bacterial amylase.View full abstractDownload PDF (500K) -
TOMOKO OHNISHI, TAKESHI MORI1960 Volume 48 Issue 3 Pages 406-411
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Using whole cell suspensions of a denitrifying bacterium and P32 as a tracer, it was demonstrated that phosphorylation takes place coupling with the denitrifying reaction under the anaerobic condition.
2. The dependencies of both nitrogen evolution and phosphate incorporation on pH, length of reaction time and concentration of phosphate were investigated.
3. Soluble compounds extracted by perchloric acid were analysed by the chromatographic fractionation and it was demonstrated that along with the denitrification lasting for only 10 minutes, P32 was incorporated into almost all nucleotides appeared in the chromatogram.
4. Some intermediate steps in the denitrifying pathway were also found to evoke the process of phosphorylation.View full abstractDownload PDF (344K) -
IV. δ-AMINOVALERIC ACID-GLUTAMIC ACID TRANSAMINASEAKIRA ICHIHARA, ELIZABETH A. ICHIHARA, MASAMI SUDA1960 Volume 48 Issue 3 Pages 412-420
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. δ-Aminovaleric acid-glutamic acid transaminase was isolated from Pseudomonas and purified.
2. This enzyme catalyzes the following reaction:
δ-aminovaleric acid+α-ketoglutaric acid_??_glutaric semialdehyde+L-glutamic acid
Substrate specificity was restricted to α-aminovaleric acid and α-ketoglutaric acid. None of the several amino acids nor pyruvic acid tested were inactive. Glutaric semialdehyde was identified as the product of the forward reaction and δ-aminovaleric acid as that of the reverse reaction.
The authors wish to thank Drs. S. Akabori and T. Okuda of this Institute for generous supply of glutaric semialdehyde ethylester.View full abstractDownload PDF (509K) -
AKIRA ICHIHARA, MASANA OGATA, MASAMI SUDA1960 Volume 48 Issue 3 Pages 421-424
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A manometric method for the differential determination of L- and D-lysine has been developed, using a preparation of the acetone powder of Pseudomonas bacteria, which contains L-lysine oxidase and its racemase. The method is quite specific for lysine and gives an error of ±0.5 μmoles.
2. Using this method the fate of DL-lysine following its injection into rats was investigated. Seventy per cent of the D-lysine and less than 20 per cent of the L-lysine could be detected in the urine and non-protein contents of the body 24 hours after its injection.View full abstractDownload PDF (232K) -
MICHIO TSUKAMURA1960 Volume 48 Issue 3 Pages 425-431
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Kanamycin inhibits the incorporations of P32 into the nucleic acid and protein fractions and the incorporations of S35 into the TCA-soluble and protein (TCA-insoluble) fractions of the parent sensitive strain of Mycobacterium avium, strain Jucho.
2. The incorporations of P32 and S35 into cellular fractions of the kanamycin-resistant strain are not inhibited by kanamycin. Kanamycin-resistant strain has rapid incorporaiions of P32 and S35 into the nucleic acid and protein fractions. The RNA:DNA ratio is higher in the kanamycin-resistant strain than in the parent sensitive strain.View full abstractDownload PDF (395K) -
MOTOJI FUJIOKA, SHIRO KAKIUCHI, HITOSHI SATANI, YUKIYA SAKAMOTO1960 Volume 48 Issue 3 Pages 432-438
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. α-Ketoglutaric acid amide, one of the oxidation products of urocanic acid, is formed by a peroxidatic reaction.
2. Since α-ketoglutaric acid amide formation is inhibited by potassium cyanide and by sodium die thyldithiocarbamate, and since the inhibition by the latter compound can be reversed by the addition of a low concentration of copper, it is assumed that the peroxidatic reaction is catalyzed by a Cu-protein.
3. Iron porphyrin protein does not seem to be involved in this reaction.View full abstractDownload PDF (389K) -
KUNIO YAGI, TOSHIHARU NAGATSU1960 Volume 48 Issue 3 Pages 439-452
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The condensation products of ethylenediamine with various catechol derivatives were studied. The main condensates of adrenaline, noradrenaline, dopamine and dopa could be separated by papar chromatography or by paper electrophoresis. Absorption and fluorescence spectra and pH-fluorescence curves of these substances were different each other. These properties can be used for identification of catechol derivatives.
2. During the condensation reaction with ethylenediamine, adrenaline gives the main condensation product of noradrenaline and ethylenediamine as its side product.
3. The main condensate of noradrenaline was found to be identical with that of 3, 4-dihydroxymandelic acid or catechol. This might be important to consider the specificity of ethylenediamine method in the fluori-metric determination of catechol derivatives of biological importance.
Authors' thanks are due to Dr. M. D. Armstrong, the Fels Research Institute, Ohio, who kindly supplied 3, 4-dihydroxymandelic acid, and to Dr. T. Rametani, Tohoku University, Sendai, who kindly synthesized dopamine.View full abstractDownload PDF (763K) -
V. PROTECTIVE EFFECT OF CALCIUM ION ON THE STABILITY OF PROTEASEMASAO NOMOTO, YOSHIKO NARAHASHI, MITSURU MURAKAMI1960 Volume 48 Issue 3 Pages 453-463
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSCalcium ion acts as an essential factor for stabilizing Streptmyces griseus protease. Under conditions in which calcium ion is deficient, the enzyme was readily inactivated by the procedures of dialysis, salting out, ion-exchange resin column treatment, or heating. It was found, however, that the enzyme was highly protected from inactivation by the presence of a small amount of calcium ion during the above mentioned procedures. The enzyme was also inactivated irreversiblly by mixing it with EDTA. It seems that the active configuration of the enzyme can be maintained and denaturation prevented by combining the enzyme with calcium ion. Strontium ion also proved capable of serving as a protective ion, but not other metal ions.
In connection with the above investigations, it was found that the enzyme was adsorbed on and eluted from the cation exchange resin column in which the functional group of resin was prepared in the state of calcium form, in a good yield. This information seems to indicate that calcium ion is not only the stabilizing factor of the enzyme but also the medium of enzymeresin complex formation in resin column treatment.
The authors wish to express their thanks to Dr. T. Akahira, Dr. M. Yanagita, Prof. K. Sakaguchi, Prof. S. Akabori, and Prof. K. Okunuki for their kind gui-dance and useful suggestions. The authors are also grateful to Mr. S. Fujita for preparation of enzyme, and to Mr. H. Kawabe for his helpful suggestions on resin.
The present work was aided in part by a grant of the Scientific Research Fund of the Ministry of Education for which the authors wish to thank the Ministry.View full abstractDownload PDF (557K) -
MASARU SOGAMI, SHIGEJI TAKEMOTO, MASATERU KAWASAKI1960 Volume 48 Issue 3 Pages 464-467
Published: September 25, 1960
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (234K)
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