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Volume 45, Issue 10
Displaying 1-13 of 13 articles from this issue
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VI. HYDROLYSIS OF VARIOUS N-ACYL DL-AMINO ACIDS BY MOLD ACYLASESKIMIYO MICHI, HARUMI TSUDA1958 Volume 45 Issue 10 Pages 745-749
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The acylase activities of the enzyme preparations from Penicillium and Aspergillus on various N-acyl DL-amino acids were measured.
2. Of these acyl derivatives of some fifteen DL-amino acids tested, the acetyl derivatives of aromatic amino acids, namely, tyrosine, phenylalanine and tryptophan and those of basic amino acids, such as arginine and lysine were hydrolyzed by the both mold acylases with almost equall ease.
3. The acetyl derivatives of aliphatic amino acids, such as methionine, alanine and glutamic acid were also susceptible substrates, although the rate of hydrolysis was somewhat lower than those above.
4. Hydroxy amino acids, such as threonine and serine, were tested in form of chloroacetyl derivatives. It was found that chloroacetyl DL-threonine was rather resistant, whereas chloroacetyl DL-serine was susceptible to the acylase.
5. The acetyl derivatives of other amino acids, such as isoleucine, leucine, valine and histidine, were hydrolyzed less easily. Acetyl DL-aspartic acid was the most resistant to the acylase.
6. Co++ ion at a comcentration of 10-3, 7M accelerates the enzyme activity on various aryl DL-amino acids by about 10 to 100 per cent, with the exception that the hydrolysis of chloroacetyl DL-valine and acetyl DL-glutamic acid is inhibited.
7. Acylases from Penicillum and Aspergillus are probably the same enzyme.
The authors are grateful to Dr. J. Greenstein of National Institutes of Health, U.S.A. for generous supply of some of the acyl amino acids, to Dr. S. Tatsuoka of Takeda Pharmaceutical Industries for supplying DL-lysiee, and to Miss Isobe and Mrs. Sugimoto for performing the microanalyses. The research was aided by the Ajinomoto Company.View full abstractDownload PDF (302K) -
DAISUKE NAKADA, KEIICHI NOZU, MASAOMI KONDO1958 Volume 45 Issue 10 Pages 751-755
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn the cells of Bacillus megaterium KM, succinoxidase, p-phenylenediamine (PPDA) oxidase and oxidative activities on the several members of the tricarboxylic acid cycle are localized to the ghosts.
The similarity of the active particles derived from either intact cells or ghosts was confirmed on succinoxidase and PPDA oxidase.
Relationship between the ghosts and the active particles was discussed.View full abstractDownload PDF (326K) -
IV. STUDIES ON THE METABOLISM OF META-AMINOPHENOL IN REFERENCE TO THAT OF PARA-AMINOSALICYLIC ACIDMAKOTO NAKAO, ISAMU YANAGISAWA, HARUHISA YOSHIKAWA1958 Volume 45 Issue 10 Pages 757-762
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSMetabolism of m-aminophenol in mouse, dog and rabbit were examined by paper chromatography. N-acetylaminophenyl glucuronide, aminophenyl glucuronide, N-acetylaminophenyl sulfate, aminophenyl sulfate and an unidentified compound were excreted in the urine of mouse and rabbit. m-Aminophenyl glucuronide and m-aminophenyl sulfate were excreted in the urine of dogs given m-aminophenol. But unchanged m-aminophenol was not excreted in any case. The metabolic products of m-aminophenol were not recognized in the urine of animals to which PAS was administered, so far as the excreted urine was analysed by means of paper chromatography. These results led us to the conclusion that PAS is not metabolized through m-aminophenol in appreciable amounts.View full abstractDownload PDF (334K) -
SHIZUO WATANABE, WILLIAM SLEATOR, JR.1958 Volume 45 Issue 10 Pages 763-777
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Neither calcium nor manganese can take the place of magnesium in supplying the divalent ion requirement for pyrophosphate relaxation of glycerol-treated muscle fibers; in this respect pyrophosphate is similar to other relaxation factors of the “first” group: myokinase, the creatine-kinase system, and EDTA.
2. Cysteine causes a lengthening of contracted glycerinated fibers, which is accelerated by any one of these three bivalent cations (Mg++, Ca++ or Mn++).
The lengthening caused by cysteine is also qualitatively different in other respects from that by other relaxation factors (including pyrophosphate), and may be additive to relaxations produced by them.
3. Mono-iodoacetate has a slight accelerating effect on shortening in the ATP+Mg++ medium, it can stop cysteine lengthening, and it causes subsequent relaxation by the EDTA relaxation medium to be incomplete.
4. Old and well-washed glycerinated fibers (more than 60 days in 50 per cent glycerol-water at -10° and more than 10 hours washing in 160mM per liter KCl at 0°) relax only incompletely in the EDTA medium; this supports Ebashi's idea (6) that there is a second relaxation factor which is removed by the long preparation procedures.
5. The old well-washed fibers just described can be made to relax completely in the presence of cysteine and lower pH. However, some irreversible process is involved in such lengthening, which indicates that cysteine cannot function as the second relaxation factor.
6. DNP, KF, arsenate and arsenite have various but small inhibitory effects on the amount of shortening, but none on relaxation by EDTA.
We wish particularly to thank Dr. M. F. Morales (Naval Medical Research Institute, Bethesda, Maryland, U.S.A.) for many valuable suggestions and criticisms.View full abstractDownload PDF (973K) -
SETSURO FUJII, KIKUO ARAKAWA1958 Volume 45 Issue 10 Pages 779-783
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Some new tripeptides were synthesized and oxidized by periodic acid in a neutral medium.
2. For the selective oxidation of hydroxyamino acid residue in tripeptide, its amino group must be free.
3. The length of the other residue combined with the amino group of a hydroxyamino acid residue was inverse to the oxidizability of the peptide.
4. Free or not free of its carboxyl group of a hydroxyamino acid residue was independent to the oxidizability of the peptide.
The authors are indepted to Dr. R. Hirohata for his valuable advices and encouragement.View full abstractDownload PDF (256K) -
TANEAKI HIGASHI1958 Volume 45 Issue 10 Pages 785-793
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSPseudomonas aeruginosa contains besides P-cytochrome oxidase, an enzyme which can be extracted in a water-soluble state and which oxidizes hydro-quinone, L-ascorbate and p-phenylenediamine (the rate decreasing in this order) without addition of any cofactor. This enzyme was purified about 19 fold starting from an extract of acetone-powder of the cells. The most purified preparation had no cytochrome-like absorption spectrum and could not oxidize reduced P-cytochrome551 or reduced P-blue protein, the sub-strates which are oxidized by P-cytochrome oxidase. Unlike P-cytochrome oxidase, oxidation of hydroquinone by this enzyme is scarcely influenced by cyanide or carbon monoxide. Increase of oxygen tension up to 100 per cent results in a gradual increase in the oxidative rate.
This enzyme was tentatively named Pseudomonas hydroquinone oxidase, since hydroquinone was the most rapidly oxidized of the substrates tested and since its true biological function is not yet known.
The author would like to express his thanks to Prof. K. Okunuki and Dr. T. Horio for their valuable guidance. Thanks are also due to his colleagues Messrs. M. Nozaki, T. Yamanaka, J. Yamashita and H. Mizushima of the same laboratory for their help and discussion and Messrs. M. Nakai and K. Kusai of Ama-gasaki Factory of Nagase & Co., Ltd., for mass-culture of the microörganisms.View full abstractDownload PDF (509K) -
KAZUO OKUNUKI, KOZO IWASA, FUMIO IMAMOTO, TADAYOSHI HIGASHIYAMA1958 Volume 45 Issue 10 Pages 795-798
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBy an application of gradient elution system of anion exchange chro-matography, acid-soluble nucleotides of Aspergillus oryzae were examined.
The nucleotides which have been universally found in yeast cells and animal tissues, exist also in the fungal cells ; CMP, AMP, UMP, CDP, ADP, CTP, ATP, UTP, GTP, TPN, and UDP-acetyl hexosamine. And the cells contains another unknown nucleotide having uridine base. ATP, ADP, and UDPAH exist in relatively large amounts compared with the others.
The helpfull aids of Dr. Y. Takagi, Medical School of Osaka University, and of Dr. Y. Imanaga, Nara Woman's University, on the assay of acetyl hexosamine, are gratefully acknowledged.View full abstractDownload PDF (193K) -
MINORU AMANO, HIROZIK. K. KIHARA, ATUHIRO SIBATANI1958 Volume 45 Issue 10 Pages 799-802
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe radioactive contamination of deoxyribonucleic acid (DNA) in the normal liver of adult rats receiving P32 may be eliminated only by an extensive purification. It is suggested that the rate of DNA synthesis as estimated by the P32 incorporation does not exceed the mitotic rate in this organ. This is an additional evidence for the metabolic stability of DNA.View full abstractDownload PDF (237K) -
III. SOME PHYSICOCHEICAL CHARACTERISTICS AND THE DEGRADATION WITH RIBONUCLEASE AND TRYPSIN OF THE MICROSOMAL RIBONUCLEOPROTEIN PARTICLESYUTAKA TASHIRO1958 Volume 45 Issue 10 Pages 803-813
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSome physicochemical characteristics of the ribonucleprotein particles isolated from the rat liver microsomes with sodium deoxycholate were examined, and the particles were digested with ribonuclease and with trypsin to estimate the internal structure of the particles.
1. The isoelectric point of the particles was estimated to be pH 3.2-3.6 by turbidimetry. When pH of solution was kept between pH 2-9, these particles were stable and did not dissociate into the component macro-molecules. Whereas below pH 2, considerable protein was released from the particles.
2. About 80-85 per cent of ribonucleic acid of the particles was easily removed by the incubation at 37° for 20 minutes with pancreatic ribonuclease. The removal of nucleic acid resulted in the turbidity increase of the solution probably due to the mutual aggregateon of the particles.
3. Trypsin digested about 30-50 per cent protein of the particles at 37° within 20 minutes. When the ribonucleoprotein particles previously labeled with C14-leucine was digested with trypsin, the radioactivity per unit weight of protein decresed remarkably with time.
4. Ultracentrifugal studies demonstrated that the core nucleic acid, which was resistant th ribonuclease, was sedimented by centrifugation at 105, 000×g. for 120 minutes. Therefore the core nucleic acid is probably not a small polymucleotide as suggested by Novikoff, but a macromolecular one, and is either covered by protein as in the case of tobacco mosaic virus or is firmly combined with basic protein as in the case of nucleic acid-protamin complex.
Trypsin destructed the particles into smaller fragments, which were not sedimented by the same centrifugal forces.
5. The protein part of the ribonucleoprotein obtained by the incubation with ribonuclease was hardly soluble to Miller-Golder's buffer of pH 2-9 and its maximum turbidity was at pH 5-6. This protein combines easily with yeast ribonucleic acid, and the combination of the both resulted in the turbidity increase in acidic region (pH 2-5) and the turbidity decrease in neutral region (pH 6-8).
5. From these findings there appears no doubt that a considerable part of ribonucleic acid exist on the surface of the particles to give them the negative charge, which is probably the most important factor for the stability of the particles. Further it was estimated that there existed the stable nucleoprotein in the core of the particles, of which metabolic activity was far less active than the surface.
The author wishes to express his thanks to Prof. K. Sasagawa and to Prof. A. Inouye for their encouragement.View full abstractDownload PDF (537K) -
II. FURTHER STUDY ON PROTEINASE DIGESTION OF BAKER'S YEAST CYTOCHROME CMITSUHIRO NOZAKI, HIROSHI MIZUSHIMA, TAKEKAZU HORIO, KAZUO OKUNUKI1958 Volume 45 Issue 10 Pages 815-823
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Yeast cytochrome c was modified by TCA-treatment and by boiling. These modified forms of cytochrome c are more susceptible to digestion by trypsin than the native form, in the following order: Oxidized, boiled yeast cytochrome c>Oxidized, TCA-treated yeast cytochrome c>Oxidized, native yeast cytochrome c>Reduced, native yeast cytochrome c>Oxidized, native bovine cytochrome c.
2. Native yeast cytochrome c in its reduced form is scarcely digested by bacterial proteinase and trypsin, while in its oxidized form is rapidly digested. The cytochrome c in its reduced form is digested after being oxidized by the catalytic action of the digested cytochrome c under aerobic, but not appreciably under anaerobic conditions.
3. Yeast cytochrome c modified by TCA-treatment or boiling shows almost the same absorption spectra as that of the native form, but when digested by bacterial proteinase and trypsin it shows spectra especially of the γ- and δ-bands which are different from those of the native form.
4. Modified yeast cytochrome c is reduced by yeast lactic dehydrogenase in the presence of lactate at almost the same initial rate as the native form, but the digested form is not reduced even under anaerobic conditions.
From these facts, the relation between the electron transfer by yeast cytochrome c and the configuration of its protein-moiety is discussed.
We would like to express our thanks to Messrs. T. Higashi, T. Yamanaka, and J. Yamashita for their help and discussion during this investigation, and to Mr. K. Fujii (Oriental Yeast Co., Ltd., Suita, Osaka, Japan) for his advices and for his supplying us with baker's yeast.View full abstractDownload PDF (535K) -
I. SUBSTRATE SPECIFICITY AND PROPERTIES OF THE ENZYMEMASAYUKI KATAGIRI, HIROO MAENO, KATSUJI HORI1958 Volume 45 Issue 10 Pages 825-832
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSHalophilic aldose dehydrogenase from halophilic Pseudomonas sp. was partially purified by fractionation with ammonium sulfate. The particle free enzyme showed typical halophilic nature in respects both to stability and to activity.
The soluble enzyme, which appeared to be specific with regard to the C-2 configuration of the aldose chain (i.e., the hydroxyl should be to the right), catalysed dehydrogenation of aldohexoses, aldopcntoses and disac-charides in the presence of 2, 6-dichlorophenolindophenol.
We are greatly indebted to Prof. F. Egami for his invaluable advice and discussion throughout the course of this work.View full abstractDownload PDF (418K) -
IRON INCORPORATION INTO HEME BY PREPARATIONS FROM RAT LIVERSHIGEKI MINAKAMI1958 Volume 45 Issue 10 Pages 833-844
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Incorporation of radioactive iron into heme was observed' by incubating the homogenate of rat liver. Heme was purified either by chroma-tography on celite column or by crystallization. The homogenates of other organs, such as kidney, brain, heart muscle, spleen and voluntary muscle had the similar activity.
2. The product of incorporation after incubating the homogenate with radioactive iron, was firmly bound to the particulate fractions. The heme in mitochondria had high rate of radioactivity. Radioactive hemeproteins were extracted by cholate after the incubation of mitochondria with radioiron. Radioactive heme existed in the fraction of 35-50 per cent ammonium sulfate saturation.
3. The activity to incorporate radioactive iron into heme was found in the particulate fraction of liver cell. The high activity was observed in mitochondrial fraction.
4. The active principle for the incorporation of iron into heme was solubilized from mitochondria with sodium cholate and purified by ammonium sulfate fractionation. The activity was found in the fraction of 50-75 per cent ammonium sulfate saturation.
5. The activity of the cholate extract had the optimum at about pH 7. The incorporation was accelerated by the addition of cysteine. Addition of protoporphyrin did not cause any increase in the incorporation. The activity was totally abolished by heat-treatment.
6. The mechanism of hemeprotein synthesis in liver cell was discussed from the above findings.
The author expresses his cordial thanks to Prof. H. Yoshikawa and Prof. Y. Yoneyama for their kind guidance and encouragement in carrying out this work. Thanks are also due to Drs. Y. Kagawa, Y. Sugita, S. Morimoto and Mr. S. Tanaka of the author's laboratory and Mr. K. Titani, H. Ishikura and K. Taka-hashi of the Department of Chemistry, Faculty of Science for their encouraging discussions.View full abstractDownload PDF (761K) -
HIROSHI MIZUSHIMA, MITSUHIRO NOZAKI, TAKEKAZU HORIO, KAZUO OKUNUKI1958 Volume 45 Issue 10 Pages 845-846
Published: October 25, 1958
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (96K)
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