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Volume 51 (1962)
- Issue 6 Pages 385-
- Issue 5 Pages 313-
- Issue 4 Pages 233-
- Issue 3 Pages 169-
- Issue 2 Pages 95-
- Issue 1 Pages 1-
Volume 51, Issue 3
Displaying 1-10 of 10 articles from this issue
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MICHIO TSUKAMURA1962Volume 51Issue 3 Pages 169-171
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Pigments of the photochromogens of “unclassified mycobacteria” could be extracted with peteroleum ether after the treatment of cells with ethanol. Partition test of the saponified pigments showed that they are epiphasic carotenoids.
2. Two pigments from the photochromogen Forbers 84 were isolated by chroma-tography, in which were used alumina as adsorbent and peteroleum ether as solvent. One was yellowish and weakly adsorbed to alumina and gave an absorption spectrum characteristic to beta-carotene. Another was reddish and strongly adsorbed to alumina and gave an absorption spectrum characteristic to lycopene.
From the photochromogen Bostrum D-35, only the beta-carotene type pigment was isolated.
Both pigments were soluble in peteroleum ether, ethyl ether, benzene and chlorform but insoluble in ethanol, methanol and water. The pigments gave a colour reaction characteristic to polyene pigments. They were optically inactive.
3. In view of the results, it is believed that the pigments of the photochromogens of “unclassified mycobacteria” mainly consist of beta-carotene and/or lycopene carotenoids.
The summary of this article was reported at the general meeting of the National Hospitals and Sana-toria held in August 1961. The author indebted to Mr. S. Mizuno for his technical assistance. He wishes to express his appreciation to Dr. E. Nakano, Biological Institute of Nagoya University, for his kind advice.View full abstractDownload PDF (182K) -
I. Abnormal Ionization of Phenolic Hydroxyl Groups and Configurational Changes in Alkaline and Urea SolutionTOSHIZO ISEMURA, AKIRA IMANISHI1962Volume 51Issue 3 Pages 172-180
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe molecular configuration of B. α-amylase, which contains neither sulfhydryl nor disulfide linkages, was studied by the spectrophotometric titration, optical rotation measurements, as well as analysis of enzymatic activity in alkaline and urea solution. In alkaline pH region up to pH 11.5 about 30 per cent of all phenolic hydroxyl groups ionize almost freely, and the molecule might be expanded reversibly to some extent at upper limit of this region. The remainder of phenolic hydroxyl groups which are masked ionizes irreversibly only above pH 11.5, caus-ing the unfolding of the molecule and the inactivation of enzyme. The enzyme is stable against relatively strong alkali, even though it has no disulfide linkages which stabilize the molecule. The unfolding of the molecular .configuration and enzymatic inactivation is apparently irreversible. However, the regeneration of activity of urea denatured enzyme, except that of alkali denatured enzyme, is achieved by removing the denaturant by dialysis, or by lowering the denaturant concentration by dilution.
The authors wish to thank Nagase Sangyo Co., Ltd. for supplies of crystalline bacterial amylase and amylose.View full abstractDownload PDF (614K) -
TATSUYA SAMEJIMA, MASAKO KAMATA, KAZUO SHIBATA1962Volume 51Issue 3 Pages 181-187
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA sedimentation study was made on the acid denaturation of bovine liver catalase in mediums of different salt concentrations. The native molecule dissociated into halves, partially between pH 3 and 4 and completely below pH 3. The sedimentation coefficient of the split product was greatly dependent upon thee salt concentration and the pH value of the medium. The coefficient of the subunit first formed near pH 4 was 4.4-6.6S and, on acidifying the solution below pH 3, the coefficient decreased to a level of 1.9-4.4S. The great drop of the coefficient on lowering pH or salt concentration was due to the unfolding of the structure of the half-size subunit and to the charge effect set forth by Pedersen. The process of dissociation was partially reversible, and a component having the same coefficient as that of the native molecule was recovered when the acidic solutions were dialysed against a buffer of pH 7.0. The results were discussed in connection with the subunit make-up of the catalase molecule, which was previously studied by the denauration with alkali and organic denaturation reagents.
The authors wish to thank Dr. T. Nagumo for his assistance in carrying out sedimentation and diffusion analyses.View full abstractDownload PDF (439K) -
YOSHIKAZU KONDO1962Volume 51Issue 3 Pages 188-192
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Paper chromatographic studies were made on the cystathionine-containing fraction obtained from silkworm and related insects. It was found that this amino acid was commonly present in the larval hemolymph of silkworm, including five races with white blood and one with yellow blood, but not in other Lepidopterous insects.
2. In silkworm larvae, S35 of injected methionine was converted to cystathionine, but not to cystine or to other sulfur-containing metabolite.
3. Antheraea pernyi having no cystathionine, on the other hand, catalyzed the conversion of S35-DL-methionine to S35-cystine, S35-taurine and, S35-sulfate.
4. From the above results, the accumulation of L-cystathionine in Bombyx mori larval hemolymph seems to be caused by an absence or very low activity of the cystathionine cleaving enzyme, cystathionase.
The author is indebted to Prof. M. Suda of the Institute for Protein Research, Osaka University for discussion and encouragement in this study.View full abstractDownload PDF (281K) -
XLII. The Synthesis of 3α, 7α, 12α-Trihydroxycoprostane-[26, 27-C14] and 3α, 7α, 12α-25-Tetrahydroxycoprostane-[26, 27-C14]HIROMASA YASHIMA1962Volume 51Issue 3 Pages 193-196
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBoth 3α, 7α, 12α-trihydroxycoprostane-[26, -27-C14] and 3α, 7α, 12α 25-tetrahydroxycoprostane-[26, 27-C14] were prepared in good yiled by a new sequence of reactions.
The author wishes to thank Prof. T. Kazuno and Assistant Prof. K. Okuda for their helpful suggestions throughout this work.View full abstractDownload PDF (203K) -
II. Delactonization of Dehydro-L-Ascorbic AcidYASUO KAGAWA, HISASHI TAKIGUCHI1962Volume 51Issue 3 Pages 197-203
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The enzymatic delactonization of dehydro-L-ascorbic acid in animal tissue was described with the assay condition without loss of resulting diketogulonic acid at pH of the physiological range.
2. The enzyme was purified, and properties including proportionality of the reaction to time and enzyme concentration, cofactor requirement, stoichiometry, inhibitors, and the absence of the reverse reaction were described. The reaction product was confirmed as 2, 3-diketo-L-gulonic acid.
3. The enzyme was possibly identical to lactonase I (aldonolactonase) in almost all the properties tested and they were not separated from each other though esterases and lactonase II (uronolactonase) were removed in the course of enzyme purification.
4. The role of this enzyme in this irreversible process of ascorbic acid catabolism and physiological findings caused by the lack of its activity in primates were discussed.
The authours express their gratitude to Prof. N. Shimazono of their laboratory for his interest and encouragement. Thanks are due to Dr. K. Yamada and Dr. M. Kawada for their valuable advices.View full abstractDownload PDF (453K) -
II. Oxidation Mechanism of Cytochrome c1 in the Presence of Cytochromes a and c1YUTAKA ORII, ICHIRO SEKUZU, KAZUO OKUNUKI1962Volume 51Issue 3 Pages 204-215
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The pH optima for the oxidation of ferrocytochrome c were found to be 5.0 in citrate-phosphate buffer, and 4.5 in acetate buffer. The oxidation of ferrocytochrome c1 has its pH optimum at 6.85 in phosphate buffer. This suggests the existence of the independent oxidation mechanisms for each of these cytochromes.
2. Cytochrome a combines with an equirnolar amount of cytochrome c to form the cytochrome oxidase complex which catalyzes the oxidation of cytochrome c. The latter reaction follows an apparent first order kinetics except for a limited time and this mechanism was discussed. A paper chromatographic examination of the complex was carried out.
The authors thank Drs. S. Takemori and J. Yamashita and Messrs I. Fuke and K. Ohnishi for their encouragement and discussion during this investigation.
Our thanks are also due to Dr. B. Hagihara for the polarographic measurement.View full abstractDownload PDF (731K) -
MASASHI NAGAHISA1962Volume 51Issue 3 Pages 216-221
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A procedure was devised for obtaining porcine blood catalase in a pure crystalline state. A relatively high yield of 180mg. pure crystalline product was obtained from 2, 600ml. of red corpuscles (about 5 liter blood).
2. Pure porcine blood catalase is characterized by a Kat-f value of 61, 500±2, 500 and contains no blue substance as prosthetic group. The molecular weight and frictional ratio were determined to be 243, 000 and 1.24, respectively.
3. On alkali-treatment at pH 12.0, the molecule of porcine blood catalase was found to split into homogeneous subunits with a molecular weight 83, 000, one-third that of the original protein. The frictional ratio of the subunit was found to be 2.20. On the basis of this finding it is inferred that the molecule of porcine blood catalase consists of three equally sized subunits.
4. The absorption spectrum of the alkalidenatured catalase was found to be markedly different from that of the native catalase. No enzymatic activity was found in this state of denaturation.
The author wishes to express his sincere gratitude to Prof. H. Tamiya, Prof. A. Takamiya and Prof. K. Shibata for their valuable advices and criticisms. Thanks are also due to Dr. T. Samejima and Dr. T. Nagumo for their assistances on ultracentrifugal and diffusion analyses.View full abstractDownload PDF (2242K) -
MAKOTO NIWA1962Volume 51Issue 3 Pages 222-230
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSHistamine sensitizing factor of Bordetella pertussis was purified from the culture supernatant.
1. Zinc acetate precipitation method was employed to concentrate HSF from the culture supernatant.
2. By DEAE cellulose chromatography, about 30-fold purification was achieved.
3. Dialysis of the concentrated preparation gave a precipitate fraction which showed high HSF activity of 37800 HSD50/mg. N. about 110-fold purification was thus attained.
4. Chemical and immunological properties of the purified HSF preparation were described.
5. It was demonstrated that HSF is an entity distinct from other cell components, such as thermolabile toxin and agglutinogen.
The present author wishes to thank Prof. Y. Kuwajima of this laboratory and Prof. F. Egami of the Department of Biochemistry and Biophysics, the University of Tokyo for their continuous guidance and encouragement in this study. Thanks are also due to Dr. K. Fukushima of the Institute for Protein Research, Osaka University for infrared spectroscopy. The author is indebted to Dr. Y. Yamadeya for his able help and to Miss C. Hoshizawa for her assistance. The expense of this study was defrayed in part by a grant from the Ministry of Education.View full abstractDownload PDF (554K) -
KUNIO YAGI, HIROSHI KONDO, JUN OKUDA1962Volume 51Issue 3 Pages 231-232
Published: March 25, 1962
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (106K)
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