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Volume 53 (1963)
- Issue 6 Pages 425-
- Issue 5 Pages 333-
- Issue 4 Pages 265-
- Issue 3 Pages 167-
- Issue 2 Pages 89-
- Issue 1 Pages 1-
Volume 53, Issue 2
Displaying 1-14 of 14 articles from this issue
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AKIKO KASAMAKI, SHOJI SASAKI, SHOICHIRO USAMI1963 Volume 53 Issue 2 Pages 89-94
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe correlation between isocitrate lyase and isocitrate dehydrogenase in Proteus vulgaris was investigated under aerobic condition.
Under aerobic and anaerobic conditions, only glyoxylic acid was identified as keto acids in citrate metabolism by sonic extract, and α-ketoglutarate was not detected unless NADP was added.
The sonic extract has an ability to oxidize citrate, isocitrate, succinate, and NADPH. Isocitrate dehydrogenase activity was also confirmed in this extract.
The oxidation of citrate was accelerated by the addition of NADP. The oxidation was inhibited almost completely by malonate and cyanide in the absence of added NADP, however, the inhibition rate was low in the presence of added NADP.
Both NADPH dehydrogenation and oxidation were not influenced by cyanide, while the dehydrogenation was inhibited remarkably by the inhibitors of flavin enzymes, i.e. chlorpromazine and benzoate.
From these results, we conclude as follows: In the sonic extract of P. vulgaris, (a) under the condition without added NADP, isocitrate is metabolized via isocitrate lyase, and the resultant succinate was oxidized by succinate oxidase system, and (b) under the condition with added NADP, isocitrate dehydrogenase is able to operate together with isocitrate lyase, and the NADPH generated is oxidized by flavin enzyme.View full abstractDownload PDF (411K) -
I. Isolation of the Proteolytically Modified Phenylazobenzoyl-Taka-amylase AHIROKO TODA, SHIRO AKABORI1963 Volume 53 Issue 2 Pages 95-101
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTaka-amylase A was resistant to the action of proteolytic enzymes, but when one mole of phenylazobenzoyl group was introduced into the enzyme derivative, phenylazo-benzoyl-taka-amylase A became susceptible to the various proteases. It was, therefore, suggested that the introduction of phenylazo-benzoyl group might alter molecular conformation of intact TAA, as also supported by the changes in specific optical rotation and reduced viscosity.
Partial degradation of PhAB-TAA by “pronase” was investigated. Proteolytically modified PhAB-TAA (M-PhAB-TAA) was iso-lated in a crystalline form and its chromatographic behavior and homogeneity were investigated with the aid of DEAE-cellulose.
The authors are grateful to Prof. K. Narita and Dr. T. Ikenaka for their kind guidances and valuable discussions through this investigation, to Dr. M. Nomoto for his generous gift of “pronase” and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.View full abstractDownload PDF (1261K) -
HIROKO TODA, SHIRO AKABORI1963 Volume 53 Issue 2 Pages 102-110
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The chromatographic examination of crystalline Taka-amylase A on the DEAE-cellulose column has shown the presence of small amount of inactive impurities. Further purification of the crystalline TAA was attempted using DEAE-cellulose column.
2. Basing on the chromatographic behavior of TAA, a simplified chromatographic preparation of homogeneous enzyme was made.
3. Direct separation of enzymes from the “Takadiastase” extract was carried out by the aid of chromatography on DEAF-cellu-lose. Alkailne protease, Taka-maltase and Taka-amylase A could be separated direct-ly.
The authors wish to express their thanks to Prof. K. Narita and Dr. T. Ikenaka for their kind guidance and valuable discussions through this investigation and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.View full abstractDownload PDF (973K) -
Tchan GI BAK, ITIRO YOSIOKA1963 Volume 53 Issue 2 Pages 111-116
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEscherichia coli and a variety of other microorganisms can reduce phenazine 5, 10-di-N-oxide to phenazine. This reduction proceeds more rapidly under anaerobic conditions and the aerobic reaction can be stimulated by various hydrogen donors. 2-Hydroxy- and 2-methoxyphenazine di-N-oxides and phenazine 5-N-oxide are also reducible by E. coli cells. The effects of pH and several inhibitors of this reduction were studied.
The authors wish to express their thanks to Dr. R. Sato of the Institute for Protein Research, University of Osaka, for his guidance and encouragements during the course of this investigation.View full abstractDownload PDF (360K) -
HIDEBUMI HAZAMA, MASAYASU KITAGAWA, YUICHI YAMAMURA1963 Volume 53 Issue 2 Pages 117-123
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAcylamino acid deacylase obtained from kidney tissue catalyzed the hydrolysis of long chain N-acylamino acids. The acyl radical most susceptible to the enzymatic hydrolysis was lauroyl or myristoyl group for valine and phenylalanine. It seems that the effect of pH on the enzyme activity for N-palmitoyl-L-aspartic acid is different from that for other palmitoyl-amino acids.View full abstractDownload PDF (468K) -
ETSUKO YOSHIDA, HAJIME TAKAHASHI, BUNJI MARUO1963 Volume 53 Issue 2 Pages 124-134
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The conditions of the fractionation of proteins and nucleic acids of Pseudomonas-P on DEAE-cellulose column chromatography and sedimentation analysis of the fractions were established.
2. Amino acids incorporation experiments revealed that the uniform protein synthesis occurred in exponentially growing cells, and a heterogeneous synthesis was observed in subcellular fraction (MgP) from Pseudomonas-P.
3. Comparison was made on DEAE-cel-lulose column chromatogram and patterns of sedimentation analysis of the fractions from exponentially growing cells and from MgP.
4. MgP synthesized two types of proteins which were eluted with lower concentrations of NaCI and 0.5N KOH, respectively. The bulk of the free proteins which usually were present in intact cells were absent in the products by MgP.
5. The nascent proteins were loosely attached to ribosomes and released upon lowering the concentration of magnesium ion in solution or upon treating them with DEAE-cellulose.
The authors wish to express their many thanks to Prof. S. Akabori, the President of the Osaka University, for his kind encouragement in this work. Thanks are also due to Mr. S. Mizuno, in this institute and Dr. H. Mitsui, Kanazawa University, for their valuable discussions and advices through this work. The authors are indebted to Miss T. Hattori of this institute for the preparation of C14-amino acids.View full abstractDownload PDF (669K) -
TAMAKO KUROZUMI, KENZO KURIHARA, YUTAKA HACHIMORI, KAZUO SHIBATA1963 Volume 53 Issue 2 Pages 135-142
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA new method for the determination of DNA concentration in solutions was developed. The method is based upon the principle that free methyl green in solution fades rapidly by addition of hydrogen peroxide, while methyl green bound to DNA does not fade. Therefore, the spectroscopic measurement of the rate of fading of a methyl green-DNA mixture gives us the concentration of free and bound dyes, from which the DNA concentration can be calculated. The new method has the advantage that the measurement can be conducted immediately after the preparation of the mixture, whereas several hours are required by other methods of using methyl green. The method was applied for the stoichiometric study of the binding of methyl green by native and heat-denatured DNA's, and the results were discussed, referring to the data previously reported for the interactions of DNA with various dyes such as aminoacridines and triphenylmethanes including methyl green.View full abstractDownload PDF (573K) -
SATOSHI NAKAMURA, TAKAO NAKAMURA, YASUYUKI OGURA1963 Volume 53 Issue 2 Pages 143-146
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAbsorption spectrum of partly reduced flavin mononucleotide in hydrochloric acid solution was analyzed and the value of the “effective semiquinone formation constant” (K) was estimated by a graphical method. By using the value of K, absorption spectrum of semiquinone was determined. It was found that flavin mononucleotide semiquinone has two absorption maxima, at 350 and 490 mlt, and that the extinction coefficients at these wavelengths are 10.0×103 (350mμ) and 9.4×103M-1cm.-1 (490mμ), respectively.
Although the K-value increased with the increasing hydrogen ion concentration, the absorption spectrum of FMN semiquinone was the same irrespective of the hydrogen ion concentration within the pH range tested.
The authors wish to express their gratitudes to Dr. T. Yamada for his valuable discussions.View full abstractDownload PDF (248K) -
I. The Purification and Some Properties of the ToxinJIRO KOYAMA, FUJIO EGAMI1963 Volume 53 Issue 2 Pages 147-154
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Streptolysin S' was purified from supernatants of resting cell suspensions of Streptococcus pyogenes in a medium with oligoribonucleotides from ribonuclease I core of yeast ribonucleic acid. By successive applica tion of zone electrophoresis and DEAE-cellulose column chromatography, purified toxin with 100, 000 HU per optical density at 260mμ was obtained with good reproducibility.
2. The purified preparation thus obtained was found to contain nucleotides and amino acids.
3. From these results, it was concluded that streptolysin S' molecule may be a complex containing both oligoribonucleotides and a peptide.
The present authors wish to express their sincere thanks to Dr. H. Ishikura for his useful discussions and Dr. Y. Homma of the Institute for Infectious Diseases, University of Tokyo for his kindness to facilitate this work.View full abstractDownload PDF (547K) -
TOSHIZO ISEMURA, TOSHIO TAKAGI, YASUAKI MAEDA, KATSUHIDE YUTANI1963 Volume 53 Issue 2 Pages 155-161
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTaka-amylase A was reduced by sodium thioglycolate in 8M urea-0.01M EDTA to give an unfolded linear polypeptide containing nine sulfhydryl groups. The destruction of the molecular structure could be reversed by the removal of thioglycolate and urea, and by subsequent air-oxidation in appropriate conditions. The obtained reduced-oxidized Taka-amylase A had about half of the original enzymatic activity, and its various pro-perties approached to those of native Taka-amylase A. The reduced-oxidized Taka-amylase A was found to be a mixture of completely renatured Taka-amylase A and partially renatured Taka-amylase A. The former was isolated by crystallization, and its various properties coincided well with those of native Taka-amylase A. This finding suggests that the informations for the secondary and tertiary structures of Taka-amylase A are contained in its primary structure.
The authors wish to express their thanks to Sankyo Co. Ltd. for a supply of “Taka-diastase Sankyo”. This work was done during tenure of the post-doctoral fellowship of the Japanese Society for the Promotion of Science for one of the authors (T. T.).View full abstractDownload PDF (1553K) -
KUNIO YAGI, TAKAYUKI OZAWA1963 Volume 53 Issue 2 Pages 162-163
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (717K) -
KEITARO HIROMI, SÔZABURO ONO1963 Volume 53 Issue 2 Pages 164-166
Published: February 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (146K) -
1963 Volume 53 Issue 2 Pages e3
Published: 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (32K) -
1963 Volume 53 Issue 2 Pages e4
Published: 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (39K)
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