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Volume 55 (1964)
- Issue 6 Pages 587-
- Issue 5 Pages 469-
- Issue 4 Pages 355-
- Issue 3 Pages 217-
- Issue 2 Pages 95-
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Volume 55, Issue 6
Displaying 1-17 of 17 articles from this issue
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I. Purification of RicinMASATSUNE ISHIGURO, TAKAO TAKAHASHI, GUNKI FUNATSU, KATSUYA HAYASHI, M ...1964 Volume 55 Issue 6 Pages 587-592
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The purification of ricin was accom-plished by column chromatography on DEAE-and CM-cellulose and subsequent crystallization. The crystalline ricin thus obtained was referred to as ricin D.
2. Ricin D was found to be homo-geneous electrophoretically and ultracentri-fugally.
3. Ricin D was also found to be homo-geneous physiologially, showing only toxicity and neither hemagglutination nor proteolysis nor non-specific protein coagulation.
4. The toxicity of ricin D, in terms of MLD48, was 0.001μg. ricin nitrogen per gram body weight of a mouse, which was about ten-fold higher than those of the previously reported preparations.
We wish to thank Dr. B. Nuki and Dr. S. Ueki, Department of Pharmacology, School of Medicine, Kyushu University, for their kind instructions and helps in carrying out toxicity experiments on mice.View full abstractDownload PDF (1132K) -
TOSHIAKI USUI, KAZUMI YAMASAKI1964 Volume 55 Issue 6 Pages 593-598
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn order to get a further knowledge about the fate of the conjugated bile acids in the course of the enterohepatic circulation, C14-labeled or unlabeled conjugated bile acids were administered intraperitoneally or intra-duodenally to rats and rabbits both furnish-ed with bile fistulas, and the bile was collect-ed and analyzed. The results obtained were as follows.
1. When the conjugated bile acid on a physiological dose level was injected intra-duodenally into the animals it was complete-ly hydrolyzed and re-conjugated with glycine or taurine in the course of the enterohepatic circulation, whereas the conjugated bile acid administered in excess was incompletely hydrolyzed and some parts were recovered unchanged.
2. Not only glycocholic and taurocholic acids-C14 but also free cholic acid-C14 were detected in the bile of fistulated rats having received glycocholic acid-24-C14 intraperitone-ally even in a physiological dose.
3. When the rats treated with streptomy-cin were injected with glycocholic acid-24-C14 intraduodenally, the pattern of the radio-active bile acids in the collected bile was similar to that obtained when it was admini-stered intraperitoneally.
These results appear to indicate that the major part of the glycocholic acid administer-ed to the rat is hydrolyzed by intestinal bacteria in the course of the enterohepatic circulation, while some parts can be hydrolyzed by a liver enzyme (glycocholase). The participation of the intestinal mucosa for hydrolyzing the conjugated bile acids was not demonstrated.View full abstractDownload PDF (363K) -
TSUYOSHI OHNISHI, SETSURO EBASHI1964 Volume 55 Issue 6 Pages 599-603
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe velocity of Ca binding of isolated sarcoplasmic reticulum was measured by a combination of the rapid flow technique and the double-beam spectrophotometry. It was found that 1.3mg. per ml. of vesicles bind 5×10-5M Ca ions within 30 msec. at 20°C in the presence of ATP. On the basis of this result the role of Ca ions in the contraction-relaxation cycle was discussed.View full abstractDownload PDF (287K) -
SETSURO EBASHI, FUMIKO EBASHI1964 Volume 55 Issue 6 Pages 604-613
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A protein component different from actin or myosin A was extracted from the residue of rabbit skeletal muscle.
2. In the presence of the component, synthetic actomyosin became very sensitive to the calcium-related actions, i.e., the syneresis-stimulating action of calucium and the relax-ing action of calcium-removing agents such as chelating agents or the physiological relax-ing factor.
3. When myosin B was treated with a low concentration of trypsin, it became in-sensitive to the relaxing action of calcium-removing agents like synthetic actomyosin. The addition of the component to the trypsin-treated myosin B recovered the sensitivity to the calcium-related actions. Essentially the same restits were obtained with myofibrils.
4. It is concluced that the nature of myosin B responsive to the calcium-related actions is due to the presence of the compo-nent in myosin B.
5. Various analyses conducted with a purified preparation of the component, i.e., the amino acid composition, the viscosity-ionic strength relationship, the binding capacity to F-actin and the sensitivity to trypsin digestion, indicated that the component resembled tropo-myosin. However, tropomyosin prepared by the routine procedures did not show the functions exhibited by the newly discovered component.
We would like to express our sincere thanks to Dr. K. Maruyama for his invaluable advice and discussions. This work is supported in part by re-search grants of the U. S. Public Health Service, AM-04810, from National Institute of Arthritis and Meta-bolic Diseases, of Rockefeller Foundation, RF 60141, and of Pharmacological Research Foundation, Tokyo.View full abstractDownload PDF (1485K) -
MAKOTO ENDO1964 Volume 55 Issue 6 Pages 614-622
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The time course of superprecipitation and the ATPase activity of actomyosin gel were measured under low concentrations of ATP in the presence of an ATP regenerating system.
2. The initial rate of increase in turbidity of an actomyosin gel suspension during the process of superprecipitation induced by ATP was proportional to the concentration of ATP, if ATP was used in a reasonably low con-centration.
3. The apparent ATPase activity of acto-myosin gel was gradually decreased during the process of superprecipitation.
4. The decrease was not observed at a low temperature or in a high concentration of ATP.
5. The result is explained by the more limited diffusion of the substrate into the contracted actomyosin gel.
6. It is concluded that the ATPase activity of actomyosin gel remains unchanged during and after the process of superprecipitation.
7. A small amount of calcium affected neither the time course of superprecipitation, nor the ATPase activity under a low con-centration of ATP.
8. Increasing the potassium or sodium concentration caused the accelerated syneresis of actomyosin gel but did not appreciably affect its ATPase activity.
The author wishes to express his thanks to Prof. H. Kumagai for his encouragement and to Prof. S. Ebashi for suggesting this work and advices. The author is also indebted to Dr. F. Julian for his, assistance in preparing this manuscript. This work was supported in part by the grant-in-aid of U. S. Public Health Service, AM-04810, from National Institute of Arthritis and Metabolic Diseases, of the Rockefeller Foundation, RF60141, and also of Pharm-acological Research Foundation.View full abstractDownload PDF (659K) -
V. The Relation of Ribosomes to Endoplasmic Reticulum during Fibroin SynthesisYOSHIAKI MIURA, HIROWO ITO, KIYOSHI SUNAGA, KEIKO IKEDA, YOICHI MORIYA ...1964 Volume 55 Issue 6 Pages 623-628
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. By density gradient centrifugation, the homegenate of the posterior silkglands was divided into 6 fractions and their protein, RNA and lipid contents were analyzed before and after an incubation at 37°C and an aging at 4°C.
2. It was demonstrated that during the incubation, ribosomes detached from endo-plasmic reticulum and thereafter, C14-glycine did not so much incorporate into the secretory protein fraction. The role of ribosomes and endoplasmic reticulum on the fibroin synthesis was discussed.View full abstractDownload PDF (460K) -
III. Polypeptide-Oligoribonucleotide Complex Nature of the ToxinJIRO KOYAMA, FUJIO EGAMI1964 Volume 55 Issue 6 Pages 629-635
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe chemical nature of streptolysin S' was studied with the purified C14-labeled toxin and the following findings were obtained.
1. The purified C14-labeled toxin was inactivated and digested by Nagarse, but neither inactivated nor digested by trypsin. This fact indicated that amino acids existed in the toxin molecule as polypeptide (or protein) susceptible to Nagarse but not to trypsin.
2. The RNase T1 digestion of the oligo-ribonucloetide portion changed the behavior of the polypeptide against a Sephadex G-75 column.
3. The pH 10.5 treatment gave a con-siderably different gel-filtration pattern from that of the native toxin.
4. The phenol treatment of the toxin removed the polypeptide moiety from most part of the oligoribonucleotides.
5. The transfer of the hemolytic activity to Tween 40 fractions was observed by the incubation of the toxin with the detergent, as Ginsburg et al. reported. Furthermore the formation of a polypeptide-Tween complex with hemolytic activity was demonstrated.
6. The toxin was precipitated by salmine sulfate and inactivated by 8M urea but neither by 6M guanidine hydrocholoride nor by 8M NaCl.
From these results, it was concluded that streptolysin S' was a polypeptide (or protein)-oligoribonucleotide complex and the former was an essential toxic component.
The present authors wish to express their sincere thanks to Mr. Y. Sokawa for his useful discussions.View full abstractDownload PDF (467K) -
I. Purification Procedures and Properties of Hemoglobins from Bullfrog and Tadpole ErythrocytesKINZABURO HAMADA, YOSHIO SAKAI, RYOITI SHUKUYA, KOOZOO KAZIRO1964 Volume 55 Issue 6 Pages 636-642
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEach of tadpole and bullfrog hemoglobins has been separated into three components with DEAE- or CM-cellulose column chromato-graphy. Comparative studies on the properties of major components were undertaken.
1. The spectrum of tadpole homoglobin is identical with that of bullfrog with the exception that the former exhibits a notch at 290mμ, whereas the latter does not.
2. Bullfrog hemoglobin has four reactive sulfhydryl groups per mole of hemoglobin, whersas tadpole hemoglobin does not.
3. Tadpole hemoglobin is much more stable than F1 for the denaturation by urea and benzoate.
4. Tadpole hemoglobin exhibits higher oxygen affinity than bullfrog hemoglobin and no Bohr effect. The heme-heme interaction is in the same magnitude for both hemoglobins.
5. N-ethylmaleimide does not influence the oxygen affinity, the heme-heme inter-action coefficient and the Bohr effect of bullfrog hemoglobin.
The authors wish to express their appreciation to Dr. M. Matsuda, Department of Biochemistry, the Jikei University School of Medicine, for the perfor-mance of ultracentrifugal analysis. This work was supported by a Grant for Scientific Research from the Ministry of Education.View full abstractDownload PDF (1217K) -
VIII. The Sedimentation of Purified Sulphatase AL. W. NICHOL, A. B. ROY1964 Volume 55 Issue 6 Pages 643-651
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A method is described for the prepa-ration of sulphatase A from ox liver.
2. The enzyme is demonstrated to be homogeneous with respect to sedimentation coefficient by two boundary analyses, those of Baldwin and of Fujita.
3. In sedimentation velocity experiments it is shown that the sedimentation coefficient of sulphatase A varies from 6 at pH 7.5 to 14 at pH 5.0.
4. This variation in s is interpreted in terms of a polymerisation reaction in which a monomer existing at pH 6.5 and above is converted to a tetramer at pH 5.5 and below.
5. The effect of the polymerisation on previous kinetic observations is briefly dis-cussed.View full abstractDownload PDF (1519K) -
IKUO YAMASHINA, KUNIHIKO IZUMI, HIDEAKI NAKA1964 Volume 55 Issue 6 Pages 652-658
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Rabbit liver homogenate was frac-tionated into nuclear, mitochondrial, micro-somal and supernatant fractions. A purified nuclear fraction was prepared by an inde-pendent procedure. The fractions were ex-amined for purity by chemical and enzymatic analysis.
2. Hexosamine and sialic acid were de-termined on the subcellular fractions with particular attention paid for sialic acid de-termination. Most of these sugars were found to be localized in mitochondria and micro-some, the contents of hexosamine and sialic acid (μg. per mg. protein) being 7.5 and 3.2 for mitochondria and 8.9 and 8.0 for micro-some respectively.
3. Contamination of the purified nuclear fraction with connective tissue was tried to be assessed by analyzing hydroxyproline and a conclusion was drawn that nuclei contain very small amounts of hexosamine and sialic acid, if any.
4. Biological importance of the intra-cellular distribution of hexosamine and sialic acid was discussed in particular connection with membranous structures of liver cells.
Support was provided by grants from the Ministry of Education, Japan.View full abstractDownload PDF (470K) -
Quelques Remarques sur le Mécanisme de la β Substitution en Présence d'Enzymes à Phosphate de PyridoxalP. FROMAGEOT, A. SENTENAC1964 Volume 55 Issue 6 Pages 659-668
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSLa phosphosérinephospholyase présente dans une fraction protéique du sac vitellin d'embryons de poule catalyse une déphos-phorylation de la phosphosérine par β éli-mination. En présence d'ions sulfure ou sulfite, cet enzyme catalyse la substitution du groupe H2PO3-O-de la phosphosérine par un groupe HS- ou HSO3-, avec forma-tion respectivement de cystéine ou d'acide cystéique. On a comparé la vitesse de la formation d'ion phosphate à partir de phos-phosérine en absence et en présence de sulfite, et parallèment la vitesse de la désulf-hydration de la cystéine, sous l'influence de la cystéine-H2S-lyase présente dans la m_??_me fraction protéique, dans des conditions ana-logues. On constate en présence de sulfite, lorsqu'une synthèse d'acide sulfonique peut avoir lieu, un accroissement de la vitesse de la formation d'ion phosphate ou sulfure à partir respectivement de phosphosérine ou de cystéine. On discute des modalités des réactions de β substitution qui puissent rendre compte d'un tel phénomène et pro-pose un mécanisme pour la β substitution des acides aminés qui dissocie β substitution et β élimination et qui s'insère dans le cadre général des mécanismes des réactions cataly-sées par le phosphate de pyridoxal décrit par Snell.View full abstractDownload PDF (724K) -
A. G. LLOYD, P. J. LARGE, ANN M. JAMES, K. S. DODGSON1964 Volume 55 Issue 6 Pages 669-676
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe injection of D-glucose-6-O-[S35]-sulphate and D-galactose-6-O-[S35]-sulphate in rats is characterised by the excretion of the larger part of the injected dose in the urine in an unchanged form accompanied by limited amounts of inorganic [S35] sulphate. Urinary excretion of ester [S35] sulphate and inorganic [S35] sulphate is also a characteristic of ex-periments in which a [S35] sulphatide is injected in rats, although in these instances a substantial portion of radioactivity is also excreted via the bile.
Evidence is presented that D-galactose is unlikely to function as an acceptor for sulphate in the biosynthesis of naturally-occurring com-pounds containing D-galactose sulphate residues.
This work has been supported by grants to A. G. L. from the Empire Rheumatism Council and the Nuffield Foundation and a grant (A1982) from the Arthritis and Metabolic Diseases Division of the U. S. Public Health Service. P. J. L. and A. M. J. are grateful to the Medical Research Council for a Research Fel-lowship and a Research Studentship respectively. The authors wish to express their thanks to Dr. H. Jatzkewitz and Dr. J. H. Austin for samples of sulphatide preparations. Finally, Professor Dodgson wishes to acknowledge the work of Professor T. Soda which first stimulated the interest of the Cardiff Laboratories in carbohydrate sulphates.View full abstractDownload PDF (648K) -
GILLIAN M. POWELL, A. G. LLOYD, P. J. LARGE, K. S. DODGSON1964 Volume 55 Issue 6 Pages 677-679
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe metabolic fate of D-glucose-6-O-[S35]-sulphate has been investigated in the mouse by means of whole body radioautography.View full abstractDownload PDF (756K) -
SHUNSUKE MIGITA, TOSHIO TAKAGI, TOSHIZO ISEMURA1964 Volume 55 Issue 6 Pages 680-681
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (802K) -
KUNIO YAGI, TAKAYUKI OZAWA1964 Volume 55 Issue 6 Pages 682-684
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (608K) -
KIHACHIRO UEHARA, TADASHI MIZOGUCHI, YOSHIKO OKADA1964 Volume 55 Issue 6 Pages 685-687
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (215K) -
TOSHIO OKAMOTO1964 Volume 55 Issue 6 Pages 688-690
Published: June 25, 1964
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (130K)
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