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Volume 50 (1961)
- Issue 6 Pages 473-
- Issue 5 Pages 377-
- Issue 4 Pages 277-
- Issue 3 Pages 167-
- Issue 2 Pages 81-
- Issue 1 Pages 1-
Volume 50, Issue 6
Displaying 1-15 of 15 articles from this issue
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HIROSHI SUGANO, IKU WATANABE1961 Volume 50 Issue 6 Pages 473-480
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The isolation methods of two groupss of native lipoproteins (having 84 and 20% lipids) from egg yolk were described.
2. Physical measurements, chemical ana-lyses, and solubility examinations were performed on these preparations.
3. Ultracentrifugal and electrophoretic studies found that each lipoprotein fraction consists of two species of lipoproteins, respectively.
4. The proportions of four lipoproteins, phosvitin, and livetins in the egg yolk were roughly estimated on the basis of the ultracentrifugal analysis.
5. The native lipoproteins obtained here were discussed comparing with the components, reported by the previous workers.
This work was supported by a grant from the Scientific Research Fund of the Ministry of Education, which is gratefully acknowledged here.View full abstractDownload PDF (4177K) -
II. Properties of Cytochrome c551 and Brown ProteinKATSUJI HORI1961 Volume 50 Issue 6 Pages 481-485
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSCytochrome cyst and a brown protein have been obtained from a denitryfying Micrococcus together with other cytochromes, that is, cytochromes b4(I), b4(II) and cytochrome 625, 553 (HdR).
Cytochrome c551 resembled closely mam-malian cytochrme c in spectroscopic and in some other properties but seemed to have a lower isoelectric poiet than mammalian cytochrome c.
Chemical nature of the brown protein is not yet clear, and no evidence for the presence of heme group has been obtained in this chromoprotein.
The authors wishes to express his gratitude to Prof. F. Egami and Dr. S. Taniguchi for their valuable and encouraging advices and to Mr. E. Itagaki for his discussion. The author also express his thanks to Nagoya Factory of Fujisawa Chemicals Co. Ltd. for the cultivation of the bacteria.View full abstractDownload PDF (326K) -
YUTAKA NAGAI1961 Volume 50 Issue 6 Pages 486-492
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Clostridium hystolyticum collagenase has been purified by use of ammonium sulfate fractionation and starch zone electrophoresis. Purified collagenase has been found to act only on collagen and gelatin and to be free from non specific proteinases and peptidases.
2. From the N- and C-terminal amino acid analysis of collagenase digest of collagen, glycine was found in more than 95 per cent of the N-termini and hydroxyproline and alanine in 55 to 70 per cent and 16 to 18 per cent respectively of the C-termini.
3. Enzymatic digest of collagen was resolved in to about 30 fractions by Dowex 50-X2 column chromatography. Two main fractions were identified as glycylprolylhydroxyproline and glycylprolylalanine respectively, and both these peptides accounted for about 25 per cent of the total mole recovery in the digest.
The auther wishes to express his thanks to Prof. H. Noda of the Department for his helpful discussion and encouragement throughout this work. The author is indebted to Dr. J. Koyama of the Department for his kind guidance and discussion in the work of collagenase preparation and to Dr. S. Miyazaki of the Institute for Infectious Diseases, University of Tokyo, for the supply of Clostridium histolyticum strain H22.View full abstractDownload PDF (578K) -
The Action of Collagenase on Synthetic PeptidesYUTAKA NAGAI1961 Volume 50 Issue 6 Pages 493-499
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Poly-(L-prolyl-L-leucyl-glycyl) synthesized as collagen model was almost completely digested with purified collagenase to prolylleucylglycylprolylleucine, glycylprolylleucine and glycylprolylleucylglycine at the ratio of 0.8, 19 and 1.0.
2. Glycyl-L-prolyl-L-leucyl-glycyl-L-proline amide synthesized as a possible simplest substrate for collagenase was easily hydrolyzed to glycylprolylleucine and glycylproline amide with the enzyme.
3. From the results obtained above, the specificity of collagenase was discussed.
The author wishes to express his thanks to Prof. H. Noda of the Department and to Prof. S. Akabori of Osaka University for their helpful discussions and guidance throughout this work. The author is indebted to Dr. S. Sakakibara of Osaka University for his kind guidance and discussion in the work of peptide synthesis.View full abstractDownload PDF (503K) -
III. Further Studies on Purification of Peroxidase and Some of Their PropertiesMASATERU SHIN, WATARU NAKAMURA1961 Volume 50 Issue 6 Pages 500-507
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. An improved method was devised for purification of peroxidase 556 and peroxidase 566 from wheat germ. These peroxidases were obtained as crystals. Their homogeneity was shown by the migration hehavior on the resin and by the ultracentrifugal behavior.
2. Peroxidase 566 was found to be a new type of peroxidases. Its absorption spectrum resembled that of b-cytochromes. Modified forms of peroxidase 566 had the absorption spectra similar to some peroxidases obtained by other investigators.
3. Although the peroxidases had proto-heme as their prosthetic group, it was suggested from their molecular weights and other properties that properties of protein portions differ distinctly from each other.
The authors express their many thanks to Prof. Okunuki, K. for his guidance and encouragement during the work and to Dr. Kakiuchi, K. and Dr. Takagi, T. for their technical guidance in the ultracentrifugal and the diffusion analysis.View full abstractDownload PDF (1537K) -
NOBUO UI, OSAMU TARUTANI1961 Volume 50 Issue 6 Pages 508-518
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAn improved method for the purification of hog thyroglobulin was presented. The preparation of thyroglobulin, which had been extracted from frozen thyroid slices and repeatedly precipitated by ammonium sulfate at a low temperature, was found to be not homogeneous, and further purification was achieved by chromatography on DEAE-cellulose. Although an ultracentrifugally homogeneous preparation has been obtained by this procedure, the yield was no more than 50 per cent. A part of 19-S thyroglobulin could not be separated from the faster sedimenting component (F-component) of 28 S present in thyroid extracts. The possible relationship between thyroglobulin and F-component was discussed.
The authors express their gratitude to Dr. T. Uchida of the University of Tokyo for communicating her unpublished data. The expense of this research was partly defrayed by a Grant in Aid of Scientific Research from the Ministry of Education, to which the author's thanks are due.View full abstractDownload PDF (1426K) -
II. Model System Effected by Ferrous Ion, Ascorbic Acid and OxygenAKIRA HANAKI, MORIZO ISHIDATE1961 Volume 50 Issue 6 Pages 519-525
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn the reaction system containing the fer-rous chelate of EDTA and oxygen, DAB can be oxidatively N-demethylated to yield MAB. Ascorbic acid, added into the above reaction mixture, can increase the rate of N-demethylation, but can display no activity in the absence of the ferrous chelate. At several hydrogen ion concentrations, the reaction rates increase as the standard redox potential difference between the ferric-ferrous chelate couple and the ascorbate-dehydroascorbate couple increases. Ascorbic acid itself may behave like a cofactor which reactivate the system. Though this model system required the presence of free oxygen, it was not clear whether oxygen derived from the atmosphere was actually incorporated into the reaction intermediate or not.
The authors wish to thank Prof. Z. Tamur a and Prof. H. Terayama for their interest in this work and for helpful discussions.View full abstractDownload PDF (450K) -
II. Effects of Inhibitors on the Transfer of Radioactivity and Role of Lipid Fraction in the Protein SynthesisYOSHIAKI MIURA, HIROWO ITO, SHIGEO TANAKA, KENHIKO MOMOSE, KIYOSHI SUN ...1961 Volume 50 Issue 6 Pages 526-532
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSStudies on the effects of inhibitors upon the transfer of radioactivity from prelabelled silkgland cell debri to particulate protein have been developed. The role of lipid fraction in the protein synthesis has also been studied and discussed.
1. At the transfer of radioactivity from prelabelled cell debris to particulate protein, RNA, DNA and deoxycholate-soluble lipoidal materials were required, whereas the addition of chloramphenicol (10-4M), nitrogen mustard (10-5M) and 2, 4-dinitrophenol (10-4M) caused no inhibitory effect upon the transfer mechanism.
2. From the time course incubations performed with minced silkglands it seems difficult to find out any particular causal relation between cell debris protein and particulate or supernate protein. And the protein-bound radioactivity in cell debris might not be associated with the transfer reaction.
3. Slices of normal and regenerating rat liver showed a relatively high incorporation of C14-amino acids in to lipid fraction compared with that of the protein fraction. However, in the tissues showing excellent protein synthesis such as silkworm's posterior silkglands and rat ascites hepatoma cells, the incorporation of C14-amino acids into lipids was by far at a lower rate than that of the protein. No initial marked uptake of radioactivity into lipid fraction was observed.
4. When the silkgland cell debris were preliminary treated by sodium deoxycholate, the transfer of radioactivity was markedly suppressed although their radioactivity was almost completely preserved.
Thus, as for the role of lipids in the protein synthesis in silkglands, it might be supposed that the lipid fraction is not a direct precursor of protein, but mediates the transfer reaction.View full abstractDownload PDF (418K) -
DAISABURO FUJIMOTO, MAKOTO ISHIMOTO1961 Volume 50 Issue 6 Pages 533-537
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Extracts of E. coli was found to reduce adenosine-3'-phospho-5'-phosphosulfate by TPNH, DPNH, methylviologen and dihydrolipoate.
2. Cytochrome c3 of Desulfovibrie desulfuricans could be also utilized as a hydrogen donor.
3. From experiments of inhibition of quinacrine and of purification, dihydrolipoate was found to be a direct hydrogen donor in PAPS reduction.
The authors should like to express their thanks to Prof. F. Egami for his valuable advices.View full abstractDownload PDF (364K) -
KOICHIRO SUMIZU, MASAKO YOSHIKAWA, SHOZO TANAKA1961 Volume 50 Issue 6 Pages 538-543
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTwo different xylanases were identified in the culture medium of Piricularia oryzae Strain No. 9. The optimum pH values of these enzymes were 8.1 and 6.4, respectively.
The optimum temperature for pH 6.4 enzyme is 45°C. It is stable between pH of 6.0 to 3.5 at 45°C and between temperatures from 0° to 40°C at pH 6.4. The Ca++ ions, 10-3M, activates this enzyme markedly, while 10-3M Zn++, Co++, Fe++ ions and 10-5M p-CMB are inhibitory. The product of the reaction is identified chromatographically as xylose.
The properties of pH 8.1 xylanase is as follows; The optimum pH is 8.1, the optimum temperature is 45°C. This enzyme is stable between pH 6.0 and pH 9.5 at 45°C, and from 0° to 50°C at the optimal pH. The activation by Ca++ ion at a concentration of 10-3M, and the inhibition by 10-3M Zn++, Co++ and Fe++ ions and 10-5M p-CMB are also observed like pH 6.4 xylanase. It seems that the latter enzyme degrades xylan to the fragments of oligosaccharides such as xylobiose and xylotriose.View full abstractDownload PDF (386K) -
KIMIKO ASANO1961 Volume 50 Issue 6 Pages 544-545
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (112K) -
TAMOTSU FURUHASHI1961 Volume 50 Issue 6 Pages 546-547
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
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TAKASHI HASHIMOTO, MASAMITI TATIBANA, YOSHINARI ISHII, HARUHISA YOSHIK ...1961 Volume 50 Issue 6 Pages 548-549
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (128K) -
Property of Lyxo-uridine 2', 3'-cyclic Phosphate as a Substrate of Ribonuclease-IATYUNOSIN UKITA, HIKOYA HAYATSU, KEIZO WAKU1961 Volume 50 Issue 6 Pages 550-552
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (186K) -
AKIO YOSHIMOTO, TARO NAKAMURA, RYO SATO1961 Volume 50 Issue 6 Pages 553-554
Published: December 25, 1961
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (152K)
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