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KIYOSHI NOSE, DEN'ICHI MIZUNO
1968 Volume 64 Issue 1 Pages
1-6
Published: July 25, 1968
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1. The degradation of DNA of
E. coli W3110 on treatment with colicin E 2 showed a lag of 10 min while the degradation of RNA by the same treatment had a lag of 30min. When
E. coli W3110 thy was used, the lags of DNA- and RNA-degradations were both 10min.
2. Trypsin [EC 3. 4. 4. 4. ] stopped these degradations when added in the lag periods. RNA-degradation could be prevented by this treatment even after DNA-degradation had started. It was deduced from this result that these two degradation processes are independent at least partly.
3. The properties of ribosomes prepared from colicin E 2-treated cells were investigated. The activity of these ribosomes for poly-U-dependent phenylalanine incorporation into hot TCA-insoluble fraction and their sedimentation patterns in sucrose density gradient centrifugation were identical with those of normal ribosomes.
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HITOSHI TAKAHASHI, SEIICHI TAKAHARA
1968 Volume 64 Issue 1 Pages
7-11
Published: July 25, 1968
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Based on the report of WEISSBACH
et al. (
1) that kynurenamine was metabolized by monoamine oxidase [EC 1. 4. 3. 4] to 4-hydroxyquinoline, the present studies show that 5-hydroxykynurenamine is converted by monoamine oxidase to 4, 6-dihydroxyquinoline, which is easily assayed because of its stability and strong fluorescence. Using the method described above, monoamine oxidase activities of various tissues may be sensitively measured.
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INEO ISHIZUKA, TAMIO YAMAKAWA
1968 Volume 64 Issue 1 Pages
13-23
Published: July 25, 1968
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The chloroform-methanol extract from
Streptococcus hemolyticus strain D-58 cells contained about 50% by weight of glycosyl glycerides, which were purified on silicic acid columns. Structures were proposed for three of them as α-kojibiosyl-(1→3)- and α-kojitriosyl-(1→3)-diglycerides, as well as a di-O-acyl derivative of α-kojibiosyl-(1→1)-glycerylphosphoryl-1'-glycerol. The deacylation product of a less polar fraction of the lipid contained at least two compounds, one of which was identified as α-glucosyl-(1→1)-glycerol. Possible existence of N-acetylglucosaminyl and N-acetylgalactosaminyl diglycerides was also demonstrated.
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KAZUTOSI NISIZAWA, SONOKO FUJIBAYASHI, YOSHIKO KASHIWABARA
1968 Volume 64 Issue 1 Pages
25-37
Published: July 25, 1968
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Two enzyme components of polymannuronide lyase were obtained from the hepatopancereas of a marine mollusc,
Dolabella auricula Solander. These lyases showed high activities toward mannuronic acidrich alginate and a short-chain polymannuronide, but not toward a short-chain polyguluronide. The degradation of alginates from various brown algae by these lyases was incomplete and the extent of their degradation seemed roughly proportional to their mannuronic acid content. From these substrates, the lyases mainly produced two kinds of diuronides and a triuronide, but no free uronic acid. On the basis of various structural analyses, these oligo-uronides were tentatively identified as a β-mannobiuronic acid, a derivative of β-mannobiuronic acid containing a double bond, and a derivative of β-mannotiuronic acid containing a double bond. The double bond seemed to be located between the C
4, and C
5 carbon atoms of the nonreducing end residue.
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TOSHIHARU NAGATSU, JOHAN B. VAN DER SCHOOT, MORTON LEVITT, SIDNEY UDEN ...
1968 Volume 64 Issue 1 Pages
39-43
Published: July 25, 1968
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An assay method was developed to permit measurement of dopamine β-hydroxylase [EC 1. 14. 2. 1] activity in a pair of adrenal glands from a single guinea pig or rabbit. By using this method, the changes of dopamine β-hydroxylase activity after various experimental procedures and during development were measured. It was found that in guinea pig adrenals dopamine β-hydroxylase and epinephrine are essentially absent at birth but reach adult values within 5 days after birth. The enzyme activity is relatively unaffected by hormones, reserpine and even severe ascorbic acid deficiency. Only two experimental procedures were found to lower dopamine β-hydroxylase activity, administration of thyroxine or benzyloxyamines. The latter are potent inhibitors of the enzyme.
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ISAMU SHIIO, HACHIRO OZAKI
1968 Volume 64 Issue 1 Pages
45-53
Published: July 25, 1968
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Partially purified NADP-specific isocitrate dehydrogenase [EC 1. 1. 1. 42] of
Brevibacterium flavum was strongly inhibited by the simultaneous addition of glyoxylate and oxalacetate at low concentrations where though each of the acids singly cause only slight inhibition. Similar inhibition was observed with NADP-specific isocitrate dehydrogenases from
Bacillus subtilis, Escherichia coli and pig heart. Although isocitrate dehydrogenase was also considerably inhibited by the non-enzymatic condensation product between glyoxylate and oxalacetate, the condensation reaction itself was not detected under the conditions of enzyme assay. Thus, it was concluded that the concerted inhibition did not involve intermediate formation of the condensation product. Inhibition by glyoxylate, glyoxylate plus oxalacetate, or the condensation product was competitive with respect to isocitrate while inhibition by oxalacetate was of mixed type. Further kinetic analysis indicated that glyoxylate or oxalacetate combines with enzyme which is bound with oxalacetate or glyoxylate, about 60, 000 times stronger than with free enzyme. The possible role of this inhibition in the metabolic control of the TCA cycle is discussed.
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KEIJI SHIKAMA
1968 Volume 64 Issue 1 Pages
55-63
Published: July 25, 1968
Released on J-STAGE: June 30, 2008
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The binding sites of bovine serum albumin for methyl orange are destroyed on denaturation with high concentrations of urea, and most of them, 14 out of 16, reform upon removal of the urea. The affinity of the binding sites formed on renaturation, however, is lower than that of the native protein for the anion in terms of the first binding constant, K
1, and also of the intrinsic binding constant, K.
The bovine serum albumin molecule can also assume different conformations on the process of renaturation in different solvents as reflected by the binding parameters, even though the protein still has the residual constraint of the 17 disulfide bonds in the denatured form under our condition.
From the thermodynamic and the spectroscopic aspects of the anion binding, the interaction of bovine serum albumin with methyl orange can be best explained in terms of binding of the anion in hydrophobic regions on the surface of the protein molecule.
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ILONA STAPRANS, KEN-ICHI ARAI, SHIZUO WATANABE
1968 Volume 64 Issue 1 Pages
65-68
Published: July 25, 1968
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The sedimentation pattern of usual preparations of the relaxing protein is a single, sharp peak, but we found a few preparations to have two peaks. Metal-chelators or sulfhydryl compounds made the two peaks into a single peak whose s
20, w (2.7mg per ml, μ_??_0.22) was exactly the same as that of the single-peak preparation (5.1 S). The relaxing protein prepared in the presence of ethylene glycol-bis (β-aminoethylether)-N, N'-tetraacetic acid contained 4.9 moles of sulfhydryl groups (SH) per 10
5g. When incubated with N-ethylmaleimide, the SH content of the relaxing protein was reduced to 1.3 moles per 10
5g, whereas the relaxing activity of the protein was affected very little.
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KEN-ICHI ARAI, SHIZUO WATANABE
1968 Volume 64 Issue 1 Pages
69-72
Published: July 25, 1968
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It is demonstrated by gel-filtration, analytical ultracentrifugation and disc gel-electrophoresis that urea can dissociate the relaxing protein preparation into at least two different protein fractions, and that a single protein component similar to the relaxing protein can be formed from troponin and tropomyosin preparations. Thus a proposal of Ebashi and Kodama that the relaxing protein is a complex of troponin and tropomyosin is supported.
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I. The Mode of Action on Partially O-Methylated Amyloses of Taka-amylase A
MAMORU FUJINAGA-ISEMURA, TOKUJI IKENAKA, YOSHIO MATSUSHIMA
1968 Volume 64 Issue 1 Pages
73-80
Published: July 25, 1968
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1. Partially O-methylated amyloses were prepared by Haworth's methylation of amylose and the action of Taka-amylase A [EC 3. 2. 1. 1] on them was examined.
2. Evidence was obtained indicating that the glucosidic bonds of methylated amyloses were hydrolyzed by Taka-amylase A, but the 2-O-and 6-O-methyl-glucosidic bonds were not attacked.
3. 6-O-Methyl-glucosyl-glucose was isolated from the digest, suggesting that a glucosidic bond adjacent to a 6-O-methyl-glucosyl residue was hydrolyzed by Taka-amylase A.
4. A greater influence by 2-O-methylation than 6-O-methylation on the susceptibility of the substrate was observed.
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MASAHIKO KODAMA, YUSAKU TAGASHIRA, CHIKAYOSHI NAGATA
1968 Volume 64 Issue 1 Pages
81-86
Published: July 25, 1968
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The interaction of 3, 4-benzopyrene, 20-methyicholanthrene, pyrene and tetracene with calf thymus deoxyribonucleoprotein was investigated
in vitro. The hydrocarbons bound to nucleoprotein were mainly recovered in the histone fraction. Isolated histone like other globular proteins, such as albumin or globulin also interacts with hydrocarbons. From the interaction of hydrocarbons with amino acids, hydrocarbons seem to combine with a hydrophobic group composed of aromatic amino acids in the protein molecule. The biological meaning of this interaction is discussed with reference to steroid hormones.
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MUTUMI MURAMATU, TOSHIO ONISHI, TOSHIO SATO, SETSURO FUJII
1968 Volume 64 Issue 1 Pages
87-91
Published: July 25, 1968
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The development of caseinolytic, fibrinolytic, and esterolytic activities from human plasminogen was examined using various amounts of crude and purified streptokinase. Streptokinase was purified by ethanol precipitation at pH 5.6.
High esterase activity (with tosyl-L-arginine methyl ester as substrate) was obtained with a catalytic amount of crude or purified streptokinase. Further addition of streptokinase resulted in only a slight increase in this elevated activity.
Fibrinolytic activity was obtained with a catalytic amount of purified streptokinase and the activity was uneffected by further addition of the enzyme.
On the other hand, the maximum caseinolytic activity was obtained with a catalytic amount of crude streptokinase and the activity decreased on further addition of streptokinase.
However, when purified streptokinase was added, no decrease of caseinolytic activity was observed. Therefore, it seemed that the observed decrease of caseinolytic activity on addition of a large amount of streptokinase was due to an inhibitor present in the crude streptokinase. This was confirmed by experiments with purified streptokinase (ethanol precipitate), combined with the ethanol supernatant. Moreover, the decrease of caseinolytic activity by a high concentration of crude streptokinase was temperature-sensitive; the lower the temperature, the higher the inhibition.
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KATSUYA HAYASHI, MASAYUKI KUGIMIYA, MASARU FUNATSU
1968 Volume 64 Issue 1 Pages
93-97
Published: July 25, 1968
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The heat stability of lysozyme [EC 3. 2. 1. 17]-substrate complex was studied by measuring the intensity of a peak in the difference spectrum of complex formation. Contrary to the fact that the lysozyme molecule is stable up to 75°C, the activity reached a maximum at 50°C, decreased markedly above this temperature, showing a shoulder at 60-75°C in the temperature-activity profile, and was greatly lost above 80°C where the conformation of the lysozyme molecule is believed to be altered. However, the intensity of the peak in the difference spectrum of the complex was linearly decreased on raising the temperature of medium. The linear decrease in the intensity was interpreted as due to a change in the density of medium. Therefore, it was inferred that the full amount of the complex is formed over the whole range of temperature examined. Thus, the loss of activity at high temperatures such as 60-70°C was ascribed to the formation of an enzyme-substrate complex difficult to be hydrolyzed.
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TETSUO HIYAMA, SAKUZO FUKUI, KAKUO KITAHARA
1968 Volume 64 Issue 1 Pages
99-107
Published: July 25, 1968
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A lactate racemase [EC 5. 1. 2. 1] was isolated and purified about 190 fold in specific activity from the sonic extract of
Lactobacillus sake. The purified preparation was almost homogeneous by ultracentrifugal and electrophoretical analyses. Characteristic properties of the enzyme were as follows: (a) absorption spectrum showed a single peak at 274 mμ, (b) molecular weight was 25, 000, (c) the enzyme did not require any additional cofactors and showed no activity of lactate dehydrogenase, (d)
Km values were 1.7×10
-2M and 8.0×10
-2M for D- and L-lactate, respectively, (e) optimal pH was 5.8-6.2, (f) an equilibrium point was at a molar ratio of 1/1 (L-isomer/D-isomer), (g) the enzyme activity was inhibited by atebrin, adenosine monosulfate, oxamate and some of Fechelating agents, (h) pyruvate and acrylate were not incorporated into lactate during the reaction, and (i) exchange reaction of hydrogen between lactate and water did not occur during the reaction.
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FUMIO WADA, HARUMI SHIMAKAWA, MASUMITSU TAKASUGI, TOSHIHIKO KOTAKE, YU ...
1968 Volume 64 Issue 1 Pages
109-113
Published: July 25, 1968
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1. Predonisolone and hydrocortisone competitively inhibited aniline hydroxylation and aminopyrine demethylation activities.
2. Addition of predonisolone or hydrocortisone to liver microsomes caused the appearance of a difference spectrum similar to that caused by aniline.
3. These steroid hormones not only inhibited the appearance of the aniline difference spectrum but also changed the shape of the spectrum.
4. The activity of aniline hydroxylation may be due to the simultaneous action of two or more enzymes, as suggested by the results on enzyme activities and difference spectra.
5. These results demonstrated that steroid hormones, like drugs, interact with the microsomal electron transport system, and the activities of the drug-metabolizing enzyme were closely related to the metabolism of steroid hormones.
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YASUSHI ABIKO, MUNEHIRO TOMIKAWA, MASAO SHIMIZU
1968 Volume 64 Issue 1 Pages
115-117
Published: July 25, 1968
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AKIRA HACHIMORI, YOSHIAKI NOSOH, NOBUHITO SONE
1968 Volume 64 Issue 1 Pages
119-121
Published: July 25, 1968
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TARO HORI, OSAMU ITASAKA, MUTSUMI SUGITA, IKUKO ARAKAWA
1968 Volume 64 Issue 1 Pages
123-124
Published: July 25, 1968
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