All issues
Volume 44, Issue 12
Displaying 1-9 of 9 articles from this issue
- |<
- <
- 1
- >
- >|
-
XIV. INHIBITORY ACTION OF 4-HYDROXY-8-METHOXY-QUINOLINE-2-CARBOXYLIC ACID, ETHEREAL SULFATE OF XANTHURENIC ACID AND KYNURENIC ACID ON THE DIABETOGENIC PROPERTY OF XANTHURENIC ACIDYAHITO KOTAKE, MURAJI KATO1957Volume 44Issue 12 Pages 787-795
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIt has been proved that 4-hydroxy-8-methoxy-quinoline-2-carboxylic acid, diethereal sulfate of xanthurenic acid and kynurenic acid act antagonistically to xanthurenic acid with regard to the diabetogenic activity.
For the development of this activity free OH group in the 8-position of quinoline ring is necessary.
In conclusion, we heartily thank Prof. Yashiro Kotake for his pertinent advice and encouragement, Prof. K. Kodama for his revision, and also heartily thank Prof. T. Sakan for his advice to synthesis of the compounds necessary for this experiment.View full abstractDownload PDF (379K) -
II. ON THE COMPACTNESS AND THE HYDRATION OF THE MOLECULETOSHIZO ISEMURA, SHIZUE FUJITA1957Volume 44Issue 12 Pages 797-805
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The hydrodynamically effective volume, Ve of Taka-amylase A was calculated according to the treatment of Scheraga and Mandelkern. It was found to be nearly equal to M_??_/N, the anhydrous volume of the protein.
2. The hydrodynamically effective volume, Ve, of some other proteins were also calculated and compared with M_??_/N values of the respective proteins. Ve is far less than M_??_/N with flexible and hydrated protein, whereas both volumes are nearly equal with rigid anhydrous protein.
3. The observed partial specific volume by density measurement of Taka-amylase A is 0.700ml./g. and markedly less than the calculated value of 0.723ml./g. by the Cohn-Edsall method. The deviation may be caused by the occurrence of prosthetic sugar groups in the interstices between polypeptide helices in the molecule without any contribution to the molecular volume.
These facts mentioned above support the view that Taka-amylase A molecule may be rigid and compact and scarcely hydrated.
In conclusion, the authors express their hearty thanks to Prof. S. Akabori and Mr. T. Ikenaka for supplying the valuable sample. The authors are also indebted to the Ministry of Education for a grant.View full abstractDownload PDF (487K) -
ISAMU SHIIO1957Volume 44Issue 12 Pages 807-817
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Some properties of the L-proline oxidizing enzyme system of the cell suspension of a halophilic Pseudomonas strain No. 101 were studied.
2. Accumulation of L-glutamic acid was shown during the oxidation of L-praline.
3. Isotopic experiments and the oxidation test for glutamic γ-semialdehyde showed that this aldehyde might not be the direct intermediate in the oxidation of L-proline by this bacterium.
The author is indebted to Prof. S. Akabori for the helpful criticism and encouragement during the course of this work, to Prof. F. Egami, Nagoya University, for the gift of the bacterial strain, to Miss T. Wad a for the gift of uniformly C14-labeled L-proline, and to Mr, T. Okuda of the Laboratory for Protein Research of Osaka University for the gift of DL-glutamic γ-semialdehyde dimethylacetal.View full abstractDownload PDF (794K) -
II. THE FORMATION OF GLUCOSAMINIC ACIDYUJIRO IMANAGA1957Volume 44Issue 12 Pages 819-826
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Intact cell of Ps. fluor. and cell-free extract of it were capable of converting GA to GAA according to the equation,
GA+1/2O2+H2O→GAA+H2O
2. From the reaction mixture by intact cell, GAA was isolated.
3. CN- and NH2OH fairly and Cu_??_ almost completely inhibited the O2-uptake.
The author takes liberty of expressing his thanks to Prof. Dr. S. Akabori of Osaka Univ. and Prof. Dr. Y. Matsushima for their kind guidance, and also to misses Y. Sekiya, S. Ogura and M. Mikami for their assistance.View full abstractDownload PDF (333K) -
YOSHITO KAZIRO1957Volume 44Issue 12 Pages 827-838
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A new spectrophotometric method suitable for determination of TDP is presented.
2. The purification procedures of apocarboxylase and alcohol dehydrogenase from baker's yeast for this purpose are described.
3. This method enables determination of 5 to 60 mμg. of TDP at 17°, and it is expected to be more sensitive when carried out at a higher temperature.
4. The presence of glucose, lactate, R-5-P, and KG did not interfere in the accurate determination of TDP by this method.
5. Thiamine did not exhibit any stimulatory effect on the reconstracted carboxylase preparation employed in this experiment.
The author wishes to express the heartful gratitude to Prof. N. Shimazono for his helpful advices and continuous encouragement.View full abstractDownload PDF (756K) -
SUSUMU HIAI, TAKAKO MORI, SEIICHI HINO, TAKESHI MORI1957Volume 44Issue 12 Pages 839-847
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Using a strain of Clostridium originally isolated from soil, the effect of partial pressure of nitrogen as substrate and hydrogen as inhibitor on the process of anaerobic nitrogen fixation was studied.
2. The rate of nitrogen fixation decreased in the presence of molecular hydrogen and the inhibition was found to be of competitive nature. No inhibition of ammonia-uptake by hydrogen was observed.
3. The Michaelis constant of the anaerobic nitrogen fixation was estimated to be about 0.03 atmosphere and the apparent dissociation constant of hydrogen-enzyme complex was found to be approximately 0.1 atmosphere. Both values are almost the same as those obtained by previous workers in aerobic nitrogen fixation.
For gas analysis in this work thanks are due to Assist. Prof. T. Koyama and Miss H. Tanaka of the Chemical Institute, Faculty of Science, Nagoya University. This work is supported in part by Grant in Aid for Scientific Research from the Ministry of Education.View full abstractDownload PDF (455K) -
YUKIYA SAKAMOTO, KENKICHI NAKAMURA, KANJI INAMORI, SHIGEHIKO IKEDA, KA ...1957Volume 44Issue 12 Pages 849-857
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Gentisic acid was confirmed to be eliminated in the urine of hereditary and experimental alcaptonuria by the paperchromatography.
2. A method of differential determination of homogentisic acid and gentisic acid in the urine was accomplished. Gentisic acid was observed to be excreted in the urine of an alcaptonuria, who eliminates ca. 7g. of the latter daily and to be increased slightly by the administration of tyrosine (2g.) to him.
3. Gentisic acid was demonstrated to appear later and to disappear earlier than homogentisic acid in the urine of prolonged ascorbic acid deficient guinea pig. Both acids increased after the administration of tyrosine and disappeared after that of ascorbic acid in the urines of the scorbutic guinea pig.
4. The formation of gentisic acid from homogentisic acid by liver extract of scorbutic guinea pig was demonstrated by means of paper-chromatography. This acid was not oxidized further by the liver ex-tract and had not any effect on the enzymatic degradation of homogentisic acid.View full abstractDownload PDF (403K) -
TOKUJI KIMURA, TAIJI SASAKAWA1957Volume 44Issue 12 Pages 859-862
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (204K) -
MASAYASU NOMURA, JUNKO HOSODA, SUSUMU NISHIMURA1957Volume 44Issue 12 Pages 863-867
Published: December 25, 1957
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (961K)
- |<
- <
- 1
- >
- >|