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Volume 66, Issue 1
Displaying 1-19 of 19 articles from this issue
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SABURO YAMAGISHI, KOJI O'HARA, TETSUO SAWAI, SUSUMU MITSUHASHI1969 Volume 66 Issue 1 Pages 11-20
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Two types of penicillin β-lactamases [EC 3.5.2.6], penicillinase238 and penicil-linase14, were isolated from E. coli harboring transmissible R factors, RGN238 and RON14 respectively, and purified mainly by means of column chromatography. Penicillinase238 belonging to type II-penicillinases was purified about 158 fold, and penicillinase14, which is one of type I-penicillinases was purified about 270 fold.
2. Isoelectric point of penicillinase238 determined by agar gel electrophoresis was 8.3, and its s20 was 2.66S. The optimal pH was around 7.6 and the optimal temperature was 30°C for the hydrolysis of benzylpenicillin.
3. With respect to penicillinase14 the isoelectric point was 5.1 and the value of s20 was 1.43S in the synthetic boundary cell. The maximal enzyme activity to benzylpenicillin was observed at 45°C and at pH 6.5.
4. The difference between the two enzymes was also revealed by the behaviors to anions like chloride and the kinetic aspects (Km, and Vmax).View full abstractDownload PDF (2005K) -
KUMIKO KAWAGUCHI, KOHEI ISHIDATE, KUNIO TAGAWA1969 Volume 66 Issue 1 Pages 21-28
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSCytochrome c peroxidase [EC 1.11.1.5] was found in anaerobically grown yeast cells as well as aerobically grown cells. The enzyme was mainly recovered in a large particulate fraction from the anaerobic yeast cells where no mitochondrion is contained. The particles containing cytochrome c peroxidase seem to be vesicular, since the enzyme was readily extractable with hypotonic treatment. Membranes of the vesicular particles were so fragile that some portion of the enzyme was recovered in the supernatant fraction. Possible occurrence of peroxisomes in yeast cells was excluded, since catalase [EC 1.11.1.5] was mainly recovered in the supernatant fraction. When cytochrome c was produced by aeration of the anaerobic cells it was invariably found in the particles together with cytochrome c peroxidase irrespective of the degree of maturation of mito-chondria. From these results it was suggested that, although no mitochondrion nor mitochondrial cytochrome is found in anaerobic yeast cells, the particles containing cytochrome c peroxidase are related to mitochondria, since the enzyme is localized in mitochondria in aerobic yeast cells.View full abstractDownload PDF (585K) -
RADHA PANT, INDIRA DYNA MORRIS1969 Volume 66 Issue 1 Pages 29-31
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe variation of active phosphorylase activity and glycogen concentration in the tissues of Philosamia ricini during larval and pupal development were studied. The optimum pH for the active phosphorylase of larval tissue was pH 7.6 at 30°C during a 30min incubation period. The enzyme phosphorylase accumulates during early larval stage, and then declines to a constant level which is maintained till pupation. The U-shaped pattern of variation of this enzyme during larval and pupal development and more or less the reverse pattern from the pupal stage till adult emergence are remarkable. Glycogen increase during this period was due to increased amylase activity and concurrent glyconeogenesis. Variation of the U-shaped pattern of change in glycogen concentration, during metamorphosis appears to be governed by the active phosphorylase activity. The changes observed were discussed in correlation with other metabolic changes.View full abstractDownload PDF (255K) -
I. Properties of Membrane ATPase and Its Solubilized FormMICHIKO ISHIDA, SHOJI MIZUSHIMA1969 Volume 66 Issue 1 Pages 33-43
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA large part of the membrane ATPase [EC 3.6.1.3] of Bacillus megaterium was solubilized by dialysis and mild treatment with alkali. The membrane ATPase was activated by Mg++ or Ca++ and stable in the cold, while the solubilized ATPase was remarkably activated by Call and inactivated by the cold. The optimum pH for the enzyme activity varied depending on the ratio of ATP to Mg++ or Ca++. The solubilized ATPase activity was distinctly stimulated by SO3--. The effects of various compounds on the enzymatic activity were studied and several differences between the properties of the membrane-bound and the solubilized ATPase were observed. Some distinct differences were also seen between the effects of dithionite, pentachlorophenol, ethanol, gramicidine, and ADP on the Mg- and Ca-ATPase activities.View full abstractDownload PDF (648K) -
I. Comparative Studies on 3, 4-Dihydroxyphenylacetate-2, 3-Oxygenase and Pyrocatechase by Electron Spin Resonance SpectroscopyHIROSHI KITA, YOSHIHIRO MIYAKE, MIYOKO KAMIMOTO, SIRO SENOH, TOSHIO YA ...1969 Volume 66 Issue 1 Pages 45-50
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSESR* studies on the role of iron in bacterial oxygenases, 3, 4-dihydroxyphenylacetate 2, 3-oxygenase [EC 1. 13.1.7] and catechol 1, 2-oxygenase [EC 1.13.1.1, pyrocatechase], demonstrated the direct participation of the iron in these enzyme reactions. 3, 4-Dihydroxyphenylacetate 2, 3-oxygenase showed no ESR signal. An ESR signal at g=4.3 appeared in the presence of substrate and oxygen, the signal disappeared after the exhaustion of oxygen. Pyrocatechase showed an ESR signal at g=4.3. It disappeared upon addition of substrate, and reappeared following the introduction of oxygen. 3, 4-Dihydroxyphenyl-acetate 2, 3-oxygenase showed ESR signals at g=2 region, Sm=1.99, 2.01, and 2.02, by the interaction with nitric oxide. The signals were not observed in the presence of substrate. Pyrocatechase showed no ESR signal with nitric oxide in the presence of substrate or dithionite. From these observations, the valency change of the bound iron during the enzyme reactions was strongly suggested. It was also suggested that the mechanism of the enzyme reaction and the state of ligands of the iron differed between these two enzymes.View full abstractDownload PDF (451K) -
SHIGERU KOBAYASHI, SHOGO ICHII1969 Volume 66 Issue 1 Pages 51-56
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Inhibitor specificity of the side-chain cleavage of cholesterol and 20α-hydroxy-cholesterol in a soluble preparation from hog adrenocortical mitochondria was examined.
2. Strong inhibition of the cholesterol side-chain cleavage was observed by 3β-hydroxyl compounds, and moderate degree of inhibition was also shown by cholestenones. However, hydrogen at C-5 position and methyl groups at C-4 position modified the inhibitory activity of the compounds.
3. No significant inhibition of cholesterol side-chain cleavage by cholesterol esters was noticed.
4. Similar pattern of the inhibition of the side-chain cleavage of 20α-hydroxy-cholesterol was observed. However, the inhibition by 5-cholesten-3β-ol-7-one and cholestenone was significantly different from that of cholesterol side-chain cleavage.
5. The inhibition of the sidechain cleavage of cholesterol and 20α-hydroxycholesterol by cholestarol and desmosterol was shown to be of a competitive type.
6. Conversion of 4-14C-cholestenone into 14C-progesterone was detected in this enzyme system, whereas 4-14C-cholestanol was not cleaved to form 14C-5a-pregnanolone.
7. Properties of cholesterol and 20α-hydroxycholesterol side-chain cleaving enzyme system were discussed.View full abstractDownload PDF (415K) -
SUMIHIRO HASE, YOSHIO MATSUSHIMA1969 Volume 66 Issue 1 Pages 57-62
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTypical 2-amino-2-deoxy-hexoses were analyzed by gas-liquid chromatography using a new procedure in which amino sugars were converted by nitrous deamination into non-nitrogeneous substances. The deamination products were reduced with borohydride and trimethylsilylated by the conventional method. Quantitative analyses performed by the proposed method of some known natural substances were described in comparison with the analytic data obtained by ion-exchange chromatography.View full abstractDownload PDF (332K) -
IV. Anomeric Form of Maltose Produced from Phenyl α-Maltoside Catalyzed by Saccharifying α-Amylase from Bacillus subtillisKEITARO HIROMI, TOSHIO SHIBAOKA, HIROYUKI FUKUBE, SÔZABURO ONO1969 Volume 66 Issue 1 Pages 63-67
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe anomer form of product maltose formed in the hydrolytic reaction of phenyl α-maltoside into phenol and maltose catalyzed by crystalline saccharifying α-amylase [EC 3.2. 1. 1] from Bacillus subtilis was determined quantitatively under the condition that the alternative pathway (hydrolysis into glucose and phenyl α-glucoside (1)) could be ignored.
The procedure involved continuous measurements of optical rotation change and of simultaneous phenol production during the reaction, which was carried out at 24.7°C, pH 5.4 and at 0.478mM substrate concentration.
It was quantitatively demonstrated that-fnaltose released from phenyl α-maltoside was exclusively of α-form, indicating that the configuration of the substrate linkage between glucose and phenyl residues was retained during the hydrolysis catalyzed by this enzyme.View full abstractDownload PDF (351K) -
KIYOMICHI HANABUSA, HISAYO KOHNO1969 Volume 66 Issue 1 Pages 69-76
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThree phosphorylase [EC 2.4. 1. 1] b isozymes were found in pig heart and isolated by chromatography on a starch column. These enzymes were designated as enzymes 1, 11 and III in the order of elution froth the column. Several of their molecular and catalytic properties were compared, and they were also compared with those of skeletal muscle enzyme.
1. A procedure for enzyme purification on a starch column was described.
2. On ultracentrifugation, all phosphorylases showed sedimentation coefficients of about 8.5S.
3. On electrophoresis, enzyme I migrated the fastest toward the anode at pH 8.5, II at an intermediate rate and III the slowest, Recombination of isozyme molecules was studied.
4. The effects of treatment with urea, heat and low temperature on the activities were examined.
5. The Michaelis constants for G1P and AMP were measured.
6. The effects of G6P and ATP on the activities were studied. G6P only inhibited enzyme I.
7. The properties of enzyme III were the same as those of skeletal muscle enzyme.View full abstractDownload PDF (534K) -
II. The Mode of Action of Taka-amylase A on O-Methyl Derivatives of Phenyl α-MaltosideMAMORU ISEMURA, TOKUJI IKENAKA, YOSHIO MATSUSHIMA1969 Volume 66 Issue 1 Pages 77-85
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSeveral specimens of a mixture of partially O-methylated derivatives of phenyl α-maltoside were prepared where O-methylated glucose residues were predominantly mono-O-methyl derivative. The enzymatic action of Taka-amylase A [EC 3.2.1.1] on these specimens was investigated, and the reaction products were detected. Among the reaction products, the following maltose derivatives were identified: 3'-O-methyl-maltose, 4'-O-methyl-maltose, 6'-O-methyl-maltose, and 4', 6'-di-O-methyl-maltose. Any maltose derivative which had O-methyl substituent on the reducing end glucose residue was never produced by the enzyme. Phenyl 2'-O-methyl-α-maltoside which was inferred to be present in a specimen, was found to be resistant to the enzymatic action. Consequently, it seemed that in the maltose moiety of a substrate molecule all the hydroxyls on the reducing end glucose residue and the 2-hydroxyl on the non-reducing end residue played important roles in the enzymatic reaction.View full abstractDownload PDF (605K) -
SHOZABURO KITAOKA, YOSHIHISA NAKANO1969 Volume 66 Issue 1 Pages 87-94
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA colorimetric method of determining minute amounts of ω-amino acids with high sensitivity, accuracy and reproducibility utilizing a modification of the Berthelot reaction is proposed, and the experiments leading to the establishment of the standard procedure are described. Sample solution (0.1 -0.3ml) is mixed with 0.2M borate buffer (0.2ml) and 6% phenol (1.0ml). After cooling in ice water and adding 7.5% sodium hypochlorite solution (0.4ml), the mixture is heated at 100°C for 10min and promptly cooled. The optical density is read at 630mμ. Most α-amino acids, except some basic ones, give no color reaction but interfere with the reaction if present in significant amounts. Primary amines, but not secondary ones, and ammonium salts also give positive reactions. Determination of the reaction velocity of pumpkin glutamate decarboxylase [EC 4.1.1.15] is reported as an example of the application of this method for biochemical studies.View full abstractDownload PDF (524K) -
MITSUO NAKAGAWA, MITSURU UCHIYAMA1969 Volume 66 Issue 1 Pages 95-97
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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IKUKO YANAGI, HIROMICHI OKUDA, SETSURO FUJII1969 Volume 66 Issue 1 Pages 99-100
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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NOBU AKAMATSU, HIROSHI MAEDA, TSUTOMU KAMIYA, YOSHIAKI MIURA1969 Volume 66 Issue 1 Pages 101-103
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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YOSHITAKE MANO, MIHOKO YOSHIDA1969 Volume 66 Issue 1 Pages 105-108
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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YOSHITAKE MANO1969 Volume 66 Issue 1 Pages 109-111
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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TOHRU MARUNOUCHI1969 Volume 66 Issue 1 Pages 113-115
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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KYOZO OGURA, TANETOSHI KOYAMA, TSUYOSHI SHIBUYA, TOKUZO NISHINO, SHUIC ...1969 Volume 66 Issue 1 Pages 117-118
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
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SHIGEKI MIZUNO, SHIGEMITSU TANO, SOICHIRO SHIRAHATA1969 Volume 66 Issue 1 Pages 119-121
Published: July 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (221K)
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