巻号一覧
44 巻, 3 号
選択された号の論文の5件中1～5を表示しています
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MASARU SOGAMI, YOSHIHIDE MOMOTANI, YASUO INOUE1957 年 44 巻 3 号 p. 137-146
発行日: 1957/03/25
公開日: 2008/11/18
ジャーナル フリーA very sensitive method for fractionating the serum-protein was investigated and called turbidometric titration by the authors. The conclusions obtained were as follows:
1. The essential point of this method lies in making use of turbi-dometric analysis combined with salting-out. Ammonium sulfate so-lution is used as a precipitant and 1 per cent NaCl solution as solvent for serum. Authors found that the concentration of the protein should be kept low and the protein-solution should contain NaCl, these being necessary to achieve reliable results.
2. The human-serum-protein was fractionated into twelve compo-nents, say, serum albumin (h, i, j, k), serum-globulin III (f, g), serum-globulin II (d, e), and serum-globulin I (a', a, b, c). Making some improvements on the first experiments, it was found that human-serum-albumin is fractured into five components (h, i, j1, j2, k), human-serum-globulin I into seven components (a', a1, a2, b1, b2, c1, c2) and rabbit-serum-globulin I into eight components.
3. Even in the case of low protein content, the turbidometric titration was performed easily without specific concentrating methods such as freezing-drying or ultrafiltration.
The authors were indebted to Professor Kyugo Sasagawa (Department of Physiology, Faculty of Medicine, Kyoto University, Kyoto) and Professor Shiro Kit a-mura (Department of Botany, Faculty of Science, Kyoto University, Kyoto). And also the authors wish to thank Professor Tsunenobu Yarnamoto, Dr. Misazo Yamamoto (Department of Quantum-Chemistry, Faculty of Science, Kyoto Uni-versity, Kyoto) and Dr. Sohei Kondo (Department of Induced Mutation, Institute of Genetics, Mishima), Assistant Professor Hiroshi Inagaki (Institute of Chemistry, Kyoto University, Takatsuki) and Dr. Fumio Sawada (Department of Chemistry, Tokyo University, Tokyo) for their excellent advices.抄録全体を表示PDF形式でダウンロード (556K) -
KAZUO SHIBATA1957 年 44 巻 3 号 p. 147-173
発行日: 1957/03/25
公開日: 2008/11/18
ジャーナル フリー1. It has been found possible to record clearly and on a large scale the absorption spectrum of protochlorophyll and its photochemical transformation products in living etiolated leaves. By this method, the kinetics of chlorophyll formation have been investigated in vivo.
2. Pro to chlorophyll α, which can be transformed by light to chlorophyll α, has its red absorption peak at 650mμ. There is also present a form of protochlorophyll a with a peak at 636mμ which is inactive. These substances, differing from each other in vivo have been designated as P 650 and P 636.
3. It was found that the immediate product of illumination of an etiolated leaf has its red absorption peak at 684mμ. This purely photochemical effect has been designated as step one and the product formed has been called C 684.
4. The second step, a dark reaction, transforms the photochemical product, C 684, to one that has its peak at about 673mμ, called C 673. This reaction is nearly completed in about 10-20 minutes.
5. The third step, also a dark reaction but slower than the second step, changes C 673 to a substance with a peak at about 677mμ, which is characteristic of chlorophyll a in living mature leaves under natural conditions. In this period, the formation of protochlorophyll a can be observed.
6. Leaves containing C 684 or C 673 when extracted give spectrain ether identical to ordinary chlorophyll a, C677.抄録全体を表示PDF形式でダウンロード (1575K) -
II. PHENYLALANINE-GLUTAMIC ACID TRANSAMINASEISAMU SHIIO1957 年 44 巻 3 号 p. 175-181
発行日: 1957/03/25
公開日: 2008/11/18
ジャーナル フリーZone electrophoresis of the crude transaminase preparation, which is almost specific to aspartic acid and phenylalanine as amino donors, has indicated the multiple nature of the enzyme system.
From balance studies of the reactants and demonstration of the reverse reaction, it was confirmed that phenylalanine-glutamate reaction catalysed by cell-free extracts of halophilic Pseudomonas strain No. 101 was a true transamination reaction.
The equilibrium constant for the glutamate-phenylalanine reaction was found to be approximately 1.5 at pH 7.0 and 37°.
The author is indebted to Prof. S. Akabori for the helpful criticism and en-couragement during the course of this work, to Prof. F. Egami of the Nagoya Uni-versity, for the gift of the bacterial strain, to Mr. H. Mitsui and Miss. T. Wada for the helpful advices concerning zone electrophoretic and paper chromatographic tech-niques respectively, and to Mr. M. Shiroishi of the Food Research Institute, the Department of Agriculture and Forestry, and Mr. S. Sakurai of the Osaka University for the gift of pyridoxal phosphate and phenylpyruvic acid respectively.抄録全体を表示PDF形式でダウンロード (391K) -
A NEW MICRODETERMINATION OF THE TOTAL QUANTITY OF CYSTEINE PLUS CYSTINE IN PROTEIN BY HYDRAZINOLYSISKAZUOKI KURATOMI, KO OHNO, SHIRO AKABORI1957 年 44 巻 3 号 p. 183-190
発行日: 1957/03/25
公開日: 2008/11/18
ジャーナル フリーA new method for the microdetermination of the total quantity of cystine plus cysteine in protein by hydrazinolysis was described. It was confirmed that hydrogen sulfide was produced specifically and quantitatively from cystine or cysteine. The total quantity of cystine plus cysteine in some proteins was determined.抄録全体を表示PDF形式でダウンロード (393K) -
THE OCCURRENCE OF PROLINE IN ADDITION TO ALANINE AS THE N-THRMINUSTOSHIO ANDO, EIKO ABUKUMAGAWA, YUTAKA NAGAI, MAKOTO YAMASAKI1957 年 44 巻 3 号 p. 191-194
発行日: 1957/03/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (194K)
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