All issues
Volume 53, Issue 1
Displaying 1-16 of 16 articles from this issue
- |<
- <
- 1
- >
- >|
-
KAZUKO IMAI, TOSHIO TAKAGI, TOSHIZO ISEMURA1963 Volume 53 Issue 1 Pages 1-6
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSHen's egg white muramidase was reduced by sodium thioglycolate in 8M urea to give an unfolded linear polypeptide having eight sulfhydryl groups. The deformation of the molecular structure could be reversed by removal of thioglycolate, dilution of urea, and air-oxidation under appropriate conditions to give completely renatured muramid-ase in a good yield. The completely renatured muramidase was isolated by crystallization, and its various properties coincid-ed well with those of native muramidase.
This finding suggests that the informations for the secondary and tertiary structures of muramidase are contained in the primary structure.
The authors wish to express their thanks to Prof. M. Funatsu and Dr. K. Hayashi of Kyushu University who supplied us glycol chitin, and to Dr. K. Harnaguchi for his kind suggestions. Our thanks are also due to Miss. H. Nishibayashi for the analysis of cysteine.View full abstractDownload PDF (1489K) -
NORIKO KATSUSHIMA, SEN-ITIROH HAKOMORI1963 Volume 53 Issue 1 Pages 7-13
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAbnomal substances accumulated in the liver of a patient died of a familial metabolic disorder were isolated. They are complexes of protein and heteropolysaccharide, composed of a large amount of glucose and a smaller amount of glucosamine and galactosamine, showing a blue iodine reaction. The iodine reaction of the native complex was diminished by digestion with peptide hydrolase and one of the fraction obtained after digestion was resistant to digestion with α-amylase.
This investigation was initiated by the proposal of Dr. T. Sano, formerly Prof. of Pediatrics, Tohoku University, and the work was continued by the kind courtesy and interest of Dr. T. Arakawa, Prof. of Pediatrics, Tohoku University, who allowed one of the authors (N. K.) to carry out cooperative experiments in the Department of Biochemistry, Tohoku Pharmaceutical School. The authors are also grateful to Dr. K. Akazaki, Prof. of Pathology, Tohoku University, for his interest and encouragement.
A part of this investigation was supported by a Grant-in-Aid for Scientific Research, Ministry of Education, which is gratefully acknowledged.View full abstractDownload PDF (1246K) -
I. Purification and SpecificityICHIRO TOIDA1963 Volume 53 Issue 1 Pages 14-17
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSMycobacterial enzyme, which decomposes acid hydrazides to hydrazine, was isolated and purified 200-500 times of purity. This preparation had no proteolytic activity and was specific for acid hydrazides.View full abstractDownload PDF (266K) -
II Inhibition by FluorideICHIRO TOIDA1963 Volume 53 Issue 1 Pages 18-22
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFluoride inhibition of partially purified hydrazidase was studied. The mode of in-hibition was reversible and competitive with the substrate. Phosphate was not essential for the inhibition. The inhibition reached to its definite level fairly rapidly. The enzyme activity was not recovered from the inhibition by the addition of metal ions, includ ing Mg2+ and Fe2+. The degree of the inhibition was smaller than other cases when benzoyl hydrazide was the substrate.View full abstractDownload PDF (276K) -
TOKURO SATO, TOMITARO FUKUYAMA, TAEKO SUZUKI, HARUHISA YOSHIKAWA1963 Volume 53 Issue 1 Pages 23-27
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Properties of trans- and cis-benzenegly-col have been studied by paper chromatography, paper electrophoresis, colour reactions and sulphate conjugating technique. The diols produce phenylsulphate, presumably through dehydration of the conjugate of them with sulphate in the supernatant of animal liver homogenate, and catechol sulphate. trans-Benzeneglycol is more easily dehydrogenated to produce catechol sulphate than the cis-diol.
2. A substance indistinguishable chromatographically and electrophoretically from traps-benzeneglycol has been found in the urine of rabbits dosed with benzene.
3. A substance, which is a glucuronide, has been found. It produces a substance indistinguishable from trans-benzeneglycol by the treatment with β-glucuronidase and turns to a stable glucuronide producing phenol by acid dydrolysis.
4. The phenylmercapturic acid precursor has been shown by paper chromatography. Incubating benzene with animal livers, a substance, which produces the phenylmercapturic acid precursor in animal kidney slices, has been found.
5. These observations have been discussed in relation to the epoxide formation in the course of the metabolism of benzene in animal body.
Many thanks are due to Prof. M. Nakajima and Dr. N. Kurihara of Kyoto University for their kind giving of benzeneglycols, and to Prof. E. Boyland and Dr. P. Sims of the Chester Beatty Research Institute, London, for their kind teaching and giving of chemicals for the experiment.View full abstractDownload PDF (416K) -
XI. Structure of Globoside, the Main Mucolipid of Human ErythrocytesTAMIO YAMAKAWA, SACHIKO YOKOYAMA, NOBUKO HANDA(née KISO)1963 Volume 53 Issue 1 Pages 28-36
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSGloboside, the main mucolipid of human erythrocytes, was purified by repeated silicic acid column chromatography. Its component fatty acids were mainly C22-C24 group, in which nervonic acid was predominating. By mild acid hydrolysis and subsequent charcoal chromatography of liberated oligosaccharide mixture, N-acetylgalactosaminoyl (1→6) galactose was isolated. After complete methylation and subsequent methanolysis, globoside yielded several methylated hexoses, which were identified by gas-liquid chromatography. These results lead to a constitutional formula of N-acetyl galactosaminoyl (1→6) galactosyl (1→4)galactosyl (1→4) glucosyl-ceramide.
The authors wish to express their gratitude to Assist. Prof. Z. Yosizawa and Assist. Prof. M. Tomoda for carbohydrate samples, to Dr. M. Kitano of Nippon Blood Bank for the supply of human erythrocytes. They are also indebted to their colleagues in this laboratory for discussion and technical assistances. The expense of this study was aided by the Scientific Fund furnished by the Ministry of Education for which they wish to thank.View full abstractDownload PDF (3857K) -
KATSUHIRA IIDA1963 Volume 53 Issue 1 Pages 37-42
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA cell-free extract of the mucous gland of Charonia lampas was demonstrated to incorporate C14-glucose into charoninsulfuric acids in the presence of ATP. ATP was required absolutely and magnesium ions were also necessary for glucose incorporating activity of the cell-free extract. No requirement for UTP was recognized. ATP could not be replaced by AMP or UTP. ATP was converted to AMP during incubation. The addition of external sulfate or charoninsulfuric acids had no effect on the incorporating activity. The incorporation of C14-glucose preceded into S-poor charoninsulfuric acid than into S-rich one. Almost all incorporating activity of the cell-free extract was found in the supernatant after centrifuged at 6000 r.p.m.
The author, wishes to express his gratitude to Prof. F. Egami of Tokyo University for his useful advice. This research was supported by grants from the Scientiffc Research Fund of the Ministry of Education and Seikagaku-kenkyusho Ltd. Some of the experiments were carried out in the Marine Biological Station of Nagoya University.View full abstractDownload PDF (385K) -
Enzymatic Oxidation of Methylhexabital 2. Reversible Oxidation of 3-Hydroxy-MethylhexabitalKEIKO TOKI, SATOSHI TOKI, HISAO TSUKAMOTO1963 Volume 53 Issue 1 Pages 43-49
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The enzyme catalyzing the reversible oxidation of 3-OH-MHB to 3-keto-MHB is located in the soluble fraction of rabbit liver.
2. NAD+ and NADP+ can function equally well as hydrogen acceptors to this enzyme.
3. It seems that coenzymes are rather firmly bound to the enzyme.
4. This enzyme is inhibited by p-chloromercuribenzoate, α, α'-dipyridyl or o-phenanthroline.
5. Pyridine nucleotides-dependent 3-OH-MHB oxidizing enzyme is activated by FAD, FMN, methylene blue, ferricyanide and menadione, and by the disulfide compounds such as glutathione (oxidized), cystine and α-lipoic acid in the presence of pyridine nucleotide, and postulate that these compounds play the role of secondary hydrogen acceptor in this enzyme system reaction.
6. The partially purified enzyme also catalyzes the reduction of 3-keto-MHB to 3-OH-MHB in the presence of NADH or NADPH.
The authors are indebted to Wakamoto Pharmaceutical Co. Ltd. for their supply of FAD and FMN. This work was supported partly by a Grant in Aid for Scientific Research provided by the Ministry of Education to which author's thanks are also due.View full abstractDownload PDF (483K) -
YOH IMAI1963 Volume 53 Issue 1 Pages 50-60
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Myo-Inositol was biosynthesized in the rat from differently labeled carbohydrate substrates and relative incorporation of isotope into inositols indicated glucose and galactose were the best precursors, suggesting that an intact 6-carbon unit serves as a precursor for inositol. n-Glucuronates, however, were not the direct precursor and the cleavage of inositol to glucuronate was not reversible.
2. C14-Distribution pattern in biosynthesized inositol, determined by three different methods, also strongly suggested that an intact 6-carbon unit converts directly to inositol and that smaller molecular units serve as precursors for inositol only after conversion to hexoses.
3. Specific incorporation of radiocarbon into inositol from glucose was higher in kidney and accessory organs than in othertissues.
Some of the initial experiments were performed in collaboration with Dr. F. Eisenberg, Jr., at the Laboratory of Biochemistry and Metabolism, National Instituse of Arthritis and Metabolic Diseases, under the direction of Dr. D. Stetten, Jr. My departure from the laboratory and his (F. E.) official trip abroad unfortunately prevented the continued collaboration, which was originally contemplated.
The author wishes to express his deep gratitude to Prof. M. Yasuda with whose encouragement this work has been continued.
The work was supported with the Damon Runyon Memorial Fund and the Tokyo Biochemical Society.View full abstractDownload PDF (739K) -
V. On the Structure of the Glycyl Chain of Bonito Insulin IIAKIRA KOTAKI1963 Volume 53 Issue 1 Pages 61-70
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Peptide fragments produced by chy-motryptic, peptic and acid partial hydrolysis of the glycyl chain of oxidized bonito insulin II were analyzed by the usual paper-chro-matographic methods after their purification with paper-electrophoresis and -chromato-graphy.
2. The presence of Tyr-CyS linkage at the 19th and 20th position was confirmed by the N-bromosuccinimide method of Witkop, too.
3. From these results the glycyl chain of bonito insulin II was concluded to possess the following partial structure:
H-Gly-Ileu-{His, Glu-Glu-CySO3H-(CySO3H, Lys, Pro, His), CySO3H, Asp, Leu}-Phe-Glu-Leu-Glu-Asp-Tyr-CySO3H-Asp (NH2)-OH.
4. Some problems on the structure relating to the hormonal activity was discussed by comparing the genetically determined differences in the chemical structure of insu-lins from different classes, fish (bonito) and mammals (cattle).
The author wishes to express his sincere thanks to Prof. K. Satake for his helpful advice and encouragement throughout this investigation. He also wishes to acknowledge Dr. Okuyama and Mrs. S. Sasakawa for their discussion, and Shimizu Seiyaku Co., Ltd., for the kind supply of bonito insulin. This work was supported in part by the grant-in-aid from the Japanese government Ministry of Education.View full abstractDownload PDF (673K) -
TOMOKO OHNISHI1963 Volume 53 Issue 1 Pages 71-79
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Formation of ATP coupled with nitrate respiration was confirmed in the sonic extract of Pseudomonas denitrificans.
2. P/2e ratio of 0.25 in the nitrate respiration was obtained with succinate as the electron donor. Lower P/2e ratio was obtained with other electron donors such as NADH, lactate, and formate.
3. Influence of various conditions of reaction, namely tonicity of the reaction medium and the concentration of Mg++, ADP, and P, on the nitrate respiration and coupled phosphorylation was studied.
4. Apparent apyrase activity was observed in the present bacterial preparation. The dephosphorylating activity was found to show a similar tendency of changes to the phos-phorylating activity on various conditions of the reaction medium.
5. In several preparations, the respiratory control was observed both in the nitrate respiration and in the oxygen respiration.
6. Some discussion on the phosphorylation coupled with bacterial respiration was presented on the basis of known mechanism of mitochondrial phosphorylation in the mammalian tissues.
The author wishes to express her sincere gratitude to Prof. T. Mori for his instruction and discussions throughout the work. The author also thanks to Prof. B. Hagihara of Osaka University for his valuable advices and discussions. Thanks are also due to Dr. T. Ohnishi of Nagoya University for his coworks, and to Mr. E. Itagaki of Osaka Univer-sity who helped the author in experiments by Cary spectrophotometer.View full abstractDownload PDF (528K) -
YUJIRO IMANAGA1963 Volume 53 Issue 1 Pages 80-83
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (178K) -
YUJIRO IMANAGA, FUMIKO SAITO, YUKIKO KUSUDA1963 Volume 53 Issue 1 Pages 84-85
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (95K) -
TOICHIRO HOSOYA1963 Volume 53 Issue 1 Pages 86-87
Published: January 25, 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (135K) -
1963 Volume 53 Issue 1 Pages e1
Published: 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (39K) -
1963 Volume 53 Issue 1 Pages e2
Published: 1963
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (35K)
- |<
- <
- 1
- >
- >|