巻号一覧
59 巻, 5 号
選択された号の論文の13件中1～13を表示しています
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I. Photooxidation of NAD and NADPKIHACHIRO UEHARA, TADASHI MIZOGUCHI, YOSHIKO OKADA, JUNJI KUWASHIMA1966 年 59 巻 5 号 p. 433-437
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーThe photochemical inactivation of NAD and NADP by visible light in the presence of riboflavin was investigated.
1. The photochemical inactivation of the nucleotides proceeded with irradiation time.
2. The photochemical inactivation of NADP proceeded in the same way as that of NAD.
3. Riboflavin was not required in stoichiometric amounts.
4. Optimum pH of photochemical in-activation of the nucleotides was found to be around pH 4.0.
5. Oxygen is necessary for the photo-chemical inactivation of the nucleotides.
6. The photochemical inactivation of the nucleotides in the presence of methylene blue does not occur.
The authors wish to express their thanks to Miss K. Kobayashi for her assistance in the present study.抄録全体を表示PDF形式でダウンロード (302K) -
HIROMICHI OKUDA, IKUKO YANAGI, SETSURO FUJII1966 年 59 巻 5 号 p. 438-442
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーThe mechanism of the stimulation of lipolysis by adrenaline was examined in a cell free system. The action of adrenaline was not mediated through 3', 5'-AMP. Adrenaline did not act on lipase but on endogenous fat which was free from lipase.抄録全体を表示PDF形式でダウンロード (343K) -
SADAMASA MINATO, TADASHI TAGAWA, KAZUO NAKANISHI1966 年 59 巻 5 号 p. 443-448
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーLarge-scale purification of RNase Tt from Takadiastase powder was carried out by chromatography on Duolite A-2 and DEAE-Sephadex columns. And crystals of RNase T1 were obtained from a salt free, aqueous solution at a low temperature.
The authors wish to thank Dr. K. Miura of Nagoya University for his kind encouragement and advice, and are grateful to Mr. Y. Baba for amino acid analyses.抄録全体を表示PDF形式でダウンロード (2529K) -
III. The Influence of pH on the Rates of Hydrolysis of Maltose and PanoseKEITARO HIROMI, KATSUTADA TAKAHASHI, ZEN-ICHIRO HAMAUZU, SÔZABUR ...1966 年 59 巻 5 号 p. 469-475
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリー1. The dependence of the apparent Michaelis constant Km and the apparent maximal velocity V on pH has been studied at 25°C over the pH range from 2.2 to 6.9 for the hydrolytic reaction of maltose and panose catalyzed by crystalline glue-amylase of Rh. delemar.
2. The ionization constants of the essential ionizable groups 1 and 2 of the free enzyme (uncombined with substrate), Ke1, and Ke2, have been determined for maltose and panose as substrate. The values of pKe1, and pKe2 were found to be 2.9 and 5.9, respectively, for the both substrates. The heats of ioniza-tion of the two ionizable groups have been determined for panose to be ΔH1=0kcal/mole and ΔH2=-0.8 kcal/mole. The value of ΔH2 for maltose was equal to that for panose. These results have suggested that the same ionizable groups are involved in the catalysis of the both substrates.
3. The above information, together with that obtained in the previous study on the competition between the two types of sub-strates, has enabled us to conclude that the hydrolyses of the both substrates, and hence both α-1, 4 and α-1, 6 glucosidic linkages, are catalyzed by a single (the same) active center of the enzyme.
4. From the values of pKe and OH, together with the effect of solvent on pKe the essential ionizable groups 1 and 2 of the enzyme have been considered to be both carboxyl groups, the active forms of which are COO- and COOH, respectively. The role of these ionizable groups in the reaction have been discussed.
The authors wish to acknowledge with gratitude Professor J. Fukumoto and Dr. Y. Tsujisaka of Osaka Municipal Technical Research Institute ' for their donation of the crystalline enzyme and Professor K. Shibasaki of Tohoku University for his gift of panose.抄録全体を表示PDF形式でダウンロード (482K) -
IV. Hydrolysis of IsomaltoseKEITARO HIROMI, MUTSUFUMI KAWAI, SÔZABURO ONO1966 年 59 巻 5 号 p. 476-480
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリー1. The Michaelis constant Km and the maximal velocity V have been determined for the hydrolytic reaction of isomaltose catalyzed by crystalline glut-amylase of Rh. delemer at 25°C and pH 5.1.
2. It has been found that isomaltose acts as a competitive inhibitor to the hydrolytic reaction of panose catalyzed by this enzyme, and the inhibitor constant of isomaltose Ki is equal to the Michaelis constant Km of isomaltose as substrate.
3. From the study of the influence of pH on the rate of hydrolysis of isomaltose at substrate concentration sufficiently lower than its Km value, the pKe values of the essential ionizable groups of the free enzyme involved in the hydrolysis of isomaltose have been determined to be pKe1=2.85 and pKe2=5.85, which are in good agreement with those obtained for maltose and panose as substrate.
4. The above results have confirmed that the active center of the enzyme involved in the catalytic hydrolysis of isomaltose is the same as that involved in the hydrolysis of maltose and Danose, and that both α-1, 4 and α-1, 6 glucosidic linkages are hydrolyzed by the same active center of the enzyme.
The authors gratefully acknowledge the kindness of Professor J. Fukumoto and Dr. Y. Tsujisaka of Osaka Municipal Technical Research Institute who provided the crystalline enzyme and of Professor K. Shibasaki who furnished isomaltose and panose.抄録全体を表示PDF形式でダウンロード (316K) -
TAKAO NAKAMURA, SADAYUKI SHO, YASUYUKI OGURA1966 年 59 巻 5 号 p. 481-486
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーBy using the technique of Sephadex G-100 gel filtration, the tyrosinase fraction extracted from a commercial mushroom, Agaricus bisporum (harvested in spring), was separated into two active components, which were referred to as tyrosinase-a (faster effluent) and tyrosinase-b (slower effluent). The ratio of catecholoxidase- to cresoloxidase activity was 3:1 for both of these components. Ultracen-trifugal and electrophoretic analyses revealed that the preparation of tyrosinase-b obtained was homogeneous, showing a higher value of activity/A280 than tyrosinase-a. The molecular weight of tyrosinase-b was 61, 000, containing two cuprous ion per molecule. It showed a Qo2 value of as high as 100, 000 when p-cresol was used as substrate.
The authors wish to express their gratitudes to Prof. H. Tamiya for his valuable criticism in this work. Thanks are also due to Ginsen Co., Ltd., Tokyo, for their generous supply of the mushroom used in this investigation.抄録全体を表示PDF形式でダウンロード (1152K) -
KUNIHIKO SAITO1966 年 59 巻 5 号 p. 487-494
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリー1. 10-Hydroxystearic acid, m.p., 79.5-79.8°C, was isolated from natural and ex-perimentary produced adipocere by reversed-phase column chromatography and gas chromatography.
2. The chemical structure of this acid was further reconfirmed as follows: a) the ketostearic acid, prepared from the original monohydroxystearic acid by the oxidation with chromium trioxide, was converted to the oximes, b) the mixed oximes when submitted to the Beckmann reaggangement
yielded the mixed amides, and c) methyl nonanoate, dimethyl sebacate, and n-octyl-amine were identified by gas-liquidchromato-graphy as the hydrolysis products of the amides.
The author wishes to express his appreciation to Dr. J. F. McGhie for supplying synthetic specimen of 10-hydroxystearic acid and to Dr. T. Murachi and Dr. K. Fukushima for measurement of optical rotation and infrared spectra. Elementary analyses were carried out by the Central Microanalysis Laboratory, Institute for Protein Research, Osaka, Japan.抄録全体を表示PDF形式でダウンロード (525K) -
TATSUHIKO YAGI1966 年 59 巻 5 号 p. 495-500
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーMethyl S35-sulfate, 1, 2-propanediol S35-sulfate and butanediol S35-sulfate were identified from the ethanol extract of the embryo.
Distribution of S35-sulfate ester in the developing egg was compared. Isopropyl S35-sulfate as well as other sulfate esters were found to be mainly distributed in allantois.
Minced liver from chick embryo and newly-born chick had an ability to esterify various alcohols and phenols with S35-sulfate. Ability and the extent of esterification were much higher in embryo than in newly-born chick.
Significance of the formation of isopropyl sulfate in eggs was discussed.
The author is indebted to Prof. N. Tamiya for his invaluable advice and encouragement throughout this work. Thanks are also due to Mr. H. Koreyasu and Mr. K. Terato for their skillful technical assistance.抄録全体を表示PDF形式でダウンロード (1908K) -
KAZUE OZAWA, KIICHIRO SETA, HIROSHI TAKEDA, KYOZO ANDO, HAJIME HANDA, ...1966 年 59 巻 5 号 p. 501-510
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーA new method for the preparation of tightly coupled mitochondria from rat brain is described. Care was mainly taken to extirpate brain as quickly as possible and to separate the brown fractions from the precipitate of the last 5, 000×g spin. Mito-chondria prepared by this method were superior to those obtained by other pro-cedures with respect to respiratory control ratio and respiratory rate in the presence of
ADP and inorganic phosphate. The ATPase of tightly coupled brain mitochondria was activated by 2, 4-dinitrophenol to a much greater extent and by Mg++ to a lesser extent than brain mitochondria prepared by other procedures. Furthermore, mitochondria prepared by this method also contain less amounts of an endogenous inhibitor of respiration than mitochondria prepared by the other methods.
Thanks are expressed to the Prof. B. Hagihara and Drs. K. Kawai and M. Nozaki for valuable discussions and criticisms. The authors are grateful to the Prof. J. A. Olson for advice on the preparation of the manuscript.抄録全体を表示PDF形式でダウンロード (740K) -
II. Constitution of Polysaccharides from BCG Cell WallsAKIRA MISAKI, SHIZUKO YUKAWA1966 年 59 巻 5 号 p. 511-520
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリー1. Two water soluble polysaccharides have been isolated from defatted cell walls of Mycobacterium bovis (BCG).
2. The main polysaccharide fraction ([α]25D+24.0°; molecular weight 31, 000) was serologically active and composed of n-arabinose and D-galactose in a ratio 2.5:1.0. Methylation and periodate oxidation studies showed that the polysaccharide possesses a highly branched structure and consisted mainly of 1→5-linked D-arabinofuranose and 1→4 -linked D-galactopyranose units with some of arabinose units forming non-reducing terminal ends.
3. The other polysaccharide fraction ([α]25D+143.7°) was serologically less active glycogen-type α-glucan with an average chain length of 7 D-glucose units, as revealed by the methylation and periodate oxidation techniques.
The authors wish to thank Drs. S. Tatsuoka, K. Kanazawa and F. Ohmura for their continued interest and encouragement in this work. Thanks are also due to Dr. K. Tsuchiya for preparation of BCG cells and for examination of biological activities, and to Professor F. Smith of University of Minnesota, Professor A. M. Stephen of Capetown University, Dr. B. Lindberg of Swedish Forest Products Research Laboratory, Dr. S. Tomoda of Kyoritsu College of Pharmacy and Dr. G. W. Hay of Queen's University, Canada, for their gifts of authentic specimens of various methyl sugars; also to Institute for Protein Research, Osaka, for molecular weight determination.抄録全体を表示PDF形式でダウンロード (849K) -
MASAITSU FUTAI, DEN'ICHI MIZUNO1966 年 59 巻 5 号 p. 521-523
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (215K) -
TOSHIO ASAKURA, YOKO SATO, SHIGEKI MINAKAMI, HARUHISA YOSHIKAWA1966 年 59 巻 5 号 p. 524-526
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (177K) -
KUNIO YAGI, KENTARO OKAMURA, MAKOTO NAOI, AKIRA KOTAKI1966 年 59 巻 5 号 p. 527-530
発行日: 1966/05/25
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (306K)
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