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Volume 60 (1966)
- Issue 6 Pages 609-
- Issue 5 Pages 489-
- Issue 4 Pages 345-
- Issue 3 Pages 239-
- Issue 2 Pages 103-
- Issue 1 Pages 1-
Volume 60, Issue 4
Displaying 1-22 of 22 articles from this issue
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MICHIHIRO SUGANO, ISAO CHINEN, MASAFUTO WADA1966 Volume 60 Issue 4 Pages 345-351
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe fatty acid specificity of cholesterol esterification by chicken serum, with particular reference to classes of lipoproteins, was studied in vitro. Two types of experiments were performed. In one experiment, lipoproteins were separated from serum which had been incubated with cholesterol-4-C14. In the other experiment, serum lipoproteins were first separated into its subcomponents and then incubated with cholesterol-C14.
The fatty acid specificity of the esterifying enzyme in the α-lipoprotein fraction resembled that observed in the whole serum, i.e., the high specific activity of the polyunsaturated esters and the low activity of the saturated and possibly monounsaturated esters. The specificity of the β-lipoprotein fraction differed demonstrably from that observed in the case of α-lipoproteins or whole serum. Thus, the specific activities of newly formed saturated esters of cholesterol was consistently high, suggesting probable preference of the enzyme in the β-lipoprotein fraction to form the saturated esters compared to that in the α-lipoproteins. The activity of the linoleate ester was lower in the β-lipoprotein fraction but it was only significant statistically in case when previously separated lipoproteins were incubated with cholesterol-C14.
The results again suggested the possible role of the enzyme associated with high density lipoproteins in the esterification of cholesterol by chicken serum.
The authors wish to express their gratitude to Dr. O. W. Portman, Oregon Regional Primate Research Center, Oregon, U.S.A., for his invaluable criticism during the preparation of the manuscript.View full abstractDownload PDF (535K) -
III. Studies on InhibitorsSADAMASA MINATO, TADASHI TAGAWA, KAZUO NAKANISHI1966 Volume 60 Issue 4 Pages 352-356
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe inhibitors of nonspecific adenosine deaminase [EC 3.5.4.4] from Takadiastase were studied. Except for 8-azaguanine and PCMB, the inhibitors tested were competitive. From studies on competitive inhibitors, the 6-amino group of adenine seems to be involved in the bond with the enzyme. From the result observed with Tubercidin, the nitrogen atom at the 7-position also appears to be important and from the effect of 8-azaadenine, the carbon atom at the 8-position is apparently not involved in the binding. Some steric effect of 9-substituted groups appears to play a critical role in binding, because 9-α-D-glucopyranosyladenine and Angustmycin C did not combine with the enzyme. 3-Substituted adenine compounds were inhibitors of the enzyme and 9-substituted isomers were substrates, indicating that one of the active sites of the enzyme may bind with 9-substituted groups. On the basis of the substrate specificity and the inhibitors of the enzyme the mode of binding of compounds with the enzyme was discussed.
The authors wish to thank Dr. N. Otake (Institute of Applied Microbiology, the University of Tokyo) for his kind gift of Angustmycin C and Dr. S. Shirato (Kaken-Kagaku Co., Ltd.) for kindly providing the 1'ubercidin. They should also like to thank Dr. B. Shimizu and Dr. T. Nishimura for kindly giving us adenine compounds and for helpful discussion. Thanks are also due to Mr. K. Terui for his technical assistance.View full abstractDownload PDF (352K) -
YORIKO TAKETO, AKIRA TAKETO1966 Volume 60 Issue 4 Pages 357-362
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe effect of oligoribonucleotide-streptolysin S complex (RNA-SLS) on Ehrlich ascitestumor cells were studied using a highly purified preparation.
RNA-SLS caused decrease in the turbidity of the tumor cell suspension with the release of cytoplasmic content concurrently. The lytic action of RNA-SLS was inhibited by trypan blue, methylated albumin or certain phospholipids. The tumor cells were apparently less sensitive to RNA-SLS than erythrocytes. The possible involvement of streptolysin S in the oncolytic activity of hemolytic streptococci was discussed.
We wish to express our thanks to Profs. H. Okamoto and S. Kuno for their continued encouragement and interest in this study.View full abstractDownload PDF (396K) -
YASUO TAKAHASHI, KEIKICHI MASE, SACHIKO ABE1966 Volume 60 Issue 4 Pages 363-371
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe physical and chemical analysis of pig, rabbit, guinea pig and rat cerebral cortex ribosomes has been carried out. General characteristics and activity of a cell free amino acid incorporating system consisting of cerebral cortex ribosomes and cell sap have also been investigated.
1. The schlieren sedimentation pattern of purified brain ribosomes consisted of the following peaks: 73S, 59S and lllS. The ratio O. D. 260/O. D. 235 of the purified ribosomes was 1.60, whereas the ratio O. D. 260/O. D. 235 of the ribosome pellet was 1.46.
2. For the maximal incorporation, ATP, GTP, ATP-generating system, K+, Mg++, and cell sap were required.
3. Addition of ribonuclease [EC 2.7.7.16] and puromycin inhibited the incorporation.
4. The effect of an amino acids mixture was inhibitory on the incorporation.
5. C14-Leucine was incorporated into the brain ribosomes almost linearly for 60 minutes.
6. Brain ribosomes incorporated C14-leucine more actively than brain microsomes.
7. The incorporating activity of brain ribosomes was as high as that of liver ribosomes.
8. The transfer of C14-leucyl-sRNA to brain ribosomal protein was examined. Transfer proceeded almost linearly for 30 minutes. The requirements for the maximal rate of this transfer were ATP, ATP-generating system, GTP, and cell sap. The rate of the transfer of C14-leucyl-sRNA to ribosomal protein was higher than the transfer to brain microsomal protein in a 30 minute incubation.
Authors wish to thank Dr. K. Ogata, Department of Biochemistry, Niigata University School of Medicine, Niigata, for his interest and encouragement, and Dr. H. Sugano and Miss. I. Watanabe, Department of Chemistry, Niigata University School of Science, for the ultracentrifugation analysis.View full abstractDownload PDF (1406K) -
I. Purification and Properties of PhosphodiesterasesKAZUYA TANIGUCHI, AKIRA TSUGITA1966 Volume 60 Issue 4 Pages 372-380
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA study was made of the purification and some properties of phosphodiesterases [EC 3.1.4.1] produced by B. subtilis Marburg strain. Pdase I isolated from a culture supernatant and Pdase II' isolated from cell extracts were highly purified. Comparative studies of the enzymatic and antigenic properties demonstrated that Pdase I was different from Pdase II'.
The authors wish to express their thanks to Dr. Eric A. Terzaghi for his valuable discussion. Thanks are also due to Mr. K. Takeda and Miss H. Kikkawa for their valuable discussion and for participating in the early stage of this work.View full abstractDownload PDF (556K) -
AKIRA IMANISHI1966 Volume 60 Issue 4 Pages 381-390
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. By an electrodialysis technique bacterial α-amylase [EC 3.2.1.1 B. subtilis] was freed from calcium ions. Using the calcium-depleted enzyme, significance of calcium binding in the stability and activity of the enzyme was studied and the following information was obtained.
2. Calcium ions can be removed from the enzyme without any detectable changes in protein conformation, suggesting an apparent localization of the calcium ions on the surface of the enzyme molecule. The conformation of the calcium-free enzyme is more sensitive to alterations in external environments.
3. The calcium-depleted enzyme requires the presence in the medium of at least 4 to 5 gram atoms of calcium ions per mole to restore the same degree of stability as observed for the native enzyme.
4. The enzyme possesses three equivalent and electrostatically independent sites for calcium binding; each site has a sufficient spatial structure to permit direct chelation with a calcium ion.
5. The first binding constant, kt, has a value of the order of 106 at pH 6.7. Heat of calcium binding is small and positive. A large negative value of ΔF0 for the binding process is supplied by a large positive value of T ΔS0. Since these thermodynamic features are characteristic of interactions between charged molecules, one of the groups involved in the binding seems to be a carboxylate ion.
6. These specific binding sites disappear on denaturation of the native enzyme in concentrated urea. The unfolded protein, however, binds calcium ions through much weaker and probably nonspecific interactions.
The author expresses his deep gratitude to Prof. T. Isemura for his constant guidance and to Dr. K. Hamaguchi for his helpful discussions throughout the course of this work.View full abstractDownload PDF (1326K) -
I. Preparation and Properties of a Submitochondrial Particulate Fraction from Bovine Adrenal CortexTADATOSHI KINOSHITA, SHIGEO HORIE, NORIO SHIMAZONO, TAKESHI YOHRO1966 Volume 60 Issue 4 Pages 391-404
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A mitochondrial fraction was obtained from bovine adrenal cortex by differential centrifugation. This fraction was practically free from contamination with fragmented endoplasmic reticulum under electron micro-scopic examinations. The mitochondrial frac-tion was sonicated, and a submitochondrial particulate preparation was obtained.
2. Both whole mitochondria and the sonicated fragments contained P-450 in a high concentration that was comparable to the concentration of P-450 in liver microsomes. No significant amount of cytochrome b5 nor P420 was found in the mitochondrial preparations.
3. Spectral properties of P-450 in the mitochondrial preparations from adrenal cortex were very similar to those of P450 in liver microsomes. It could combine with EIC as well as carbon monoxide, and could be reduced with NADPH under anaerobic conditions.
4. Analytical data for hemes and iron in the submitochondrial preparation were presented. The concentrations of cytochrome oxidase [EC 1.9.3.1], cytochrome c1, and cytochrome b in the sonicated mitochondria) fragments were far less compared with the equivalent preparation from rat liver mitochondria or that from heart mitochondria.
5. The steroid 11-β-hydroxylase [EC 1.14.1.6] activity could be detected with the mitochondrial preparations. The activity was sensitive to carbon monoxide but not to cyanide.View full abstractDownload PDF (1917K) -
NOBUO TANAKA, KUMIKO SASHIKATA, HIDEYO YAMAGUCHI, HAMAO UMEZAWA1966 Volume 60 Issue 4 Pages 405-410
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBottromycin A2 and its hydrazide were found to exhibit a significant activity against in vivo and in vitro protein synthesis of E. coli B. They inhibited the incorporation of C14-labeled leucine, phenylalanine and amino acid mixture into protein of the intact cells and that of C14-labeled leucine, valine, proline, lysine and phenylalanine into protein on the ribosomes with native messengers.
Polyproline synthesis with poly C was significantly inhibited by the drugs; but polyphenylalanine synthesis with poly U and polylysine synthesis with poly A were not affected.
Bottromycin A2 and its hydrazide were demonstrated to exhibit no significant effect on labeling of sRNA with C14-labeled leucine, phenylalanine and proline, but to inhibit transfer of sRNA-bound C14-proline to poly-peptide on the ribosomes with poly C.
It was observed by the sucrose density gradient analysis of the ribosomes, synthesizing polyproline with poly C, that the antibiotic inhibited C14-proline incorporation into the hot-acid-insoluble fraction but not that into the hot-acid-soluble fraction.
The results indicated that the primary action of bottromycin A2 and its hydrazide is the inhibition of protein synthesis. The site- of action may be located in some step(s) following the binding of aminoacyl-sRNA to the mRNA-ribosome complex.
The activity of the drugs is highlydependent on the base composition of messenger nucleotides.View full abstractDownload PDF (406K) -
LXXXIV. The Metabolism of Trihydroxycoprostane in Bull FrogSETSUO BETSUKI1966 Volume 60 Issue 4 Pages 411-416
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. After intraperitoneal administration of tritium labeled trihydroxycoprostane to the bull frog, the main metabolites found in bile were trihydroxycoprostanic acid, 5β-ranol and 26-deoxy-5β-ranol, and in addition, cholic acid and tetrahydroxycoprostanic acid were identified.
2. The metabolic pathway of trihydroxy-coprostane to 5-β-ranol in the bull frog was postulated as shown in Fig. 7.
The author wishes to thank Dr. T. Hoshita for his helpful suggestion throughout this work.View full abstractDownload PDF (404K) -
YOSHIO IMAI, AKIO ITO, RYO SATO1966 Volume 60 Issue 4 Pages 417-428
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Three subfractions of microsomes were obtained by differential centrifugation from the post-mitochondrial supernatant of a 0.88M sucrose homogenate of rabbit liver, and the contents of protein, phospholipid, RNA and iron in these fractions were determined.
2. The distribution of seven enzymes and two hemoproteins among the subfractions were determined, and the results were expressed in terms of specific activity or content per unit weight of phospholipid.
3. It was found that the enzymes concerned in oxidation-reduction reactions (NADH- and NADPH-cytochrome c reductases and aniline hydroxylase as well as hemoproteins (cytochrome b5 and P-450) were most concentrated in the “light” fraction. Glucose-6-phosphatase [EC 3.1.3.9], on the other hand, seemed to occur predominantly in the “heavy” fraction. Among the other hydrolases studied, ATPase [EC 3.6.1.3] and arylsulfatase C [EC 3.1.6.1] were most abundant in microsomes of “intermediate density”, whereas esterase [EC 3.1.1.2] showed a diffuse distribution.
4. These re.ults were taken as preliminary evidence for the presence in the microsomal fraction of several types of vesicles distinguishable biochemically from one another.View full abstractDownload PDF (947K) -
NOBUO TANAKA, HIDEYO YAMAGUCHI, HAMAO UMEZAWA1966 Volume 60 Issue 4 Pages 429-434
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe site of action of kasugamycin was investigated in detail with E. coli cell-free systems. The antibiotic did not exhibit any significant effects on leucyl- and phenylalanyl-sRNA formation, but slightly affected amino-acylation of sRNA with lysine and arginine.
Incorporation of sRNA-bound phenyl-alanine or lysine into polypeptide with poly U or poly A were significantly inhibited by the presence of kasugamycin. The antibiotic was observed to exhibit a significant inhibition of polyphenylalanine or polylysine synthesis with the poly U- or poly A-attached ribosomes. The binding of phenylalanyl-sRNA to the poly U-ribosome complex was markedly in-hibited by kasugamycin.
The results indicated that the major site of action of kasugamycin is localized in the process of binding aminoacyl-sRNA with the messenger-ribosome complex.
Denatured DNA-directed polypeptide synthesis was not significantly affected by the presence of kasugamycin, which was observed to inhibit neomycin-stimulated, DNA-directed polypeptide synthesis.View full abstractDownload PDF (375K) -
VI. Occurrence of 3-O-Methylfucose in Corbicula GlycolipidOSAMU ITASAKA1966 Volume 60 Issue 4 Pages 435-438
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe neutral sugar components of a corbicula glycolipid, GL-2, were investigated and the presence of 3-O-methylfucose, xylose, mannose and glucose was shown by gas chromatographic analysis. It was found that GL-2 and GL-3 had a high hemagglutination inhibition activity with eel serum.
The author acknowledges the valuable discussion and suggestion of Prof. T. Hori of this laboratory and Prof. T. Yamakawa, the University of Tokyo, during the course of this investigation. The author also wishes to express thanks to Dr. G. F. Springer of Northwestern University for the hemagglutination inhibition test and to Dr. J. Okano of Daiichi Seiyaku Co., Ltd. for the gift of Digitalium serum.View full abstractDownload PDF (251K) -
Number-Average Molecular Weights of Various Fractions of Amylose Determined by Using Gluc-amylase of Rhizopus delemarKEITARO HIROMI, KÔZO OGAWA, NORITO NAKANISHI, SÔZABURO ONO1966 Volume 60 Issue 4 Pages 439-449
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A theory has been developed which describes the time course of exo-enzyme-catalyzed hydrolysis of linear high polymer substrates which is accompanied by a competitive inhibition by products. The theory predicts that there is a linear relationship between t/p and p, where p is the concentration of product at time t, and that the slope s of the plot of t/p versus p is proportional to the number-average molecular weight _??_Mn of the polymer substrate when a given amount of substrate is taken. Based on this proportionality between s and -Mn, a kinetic method was proposed to determine the number-average molecular weight of linear polymer substrate by using an exo-enzyme hydrolyzing the polymer.
2. The theory was applied to the hydrolytic reactions of various fractions of amylose of different degrees of polymerization catalyzed by crystalline exo-enzyme glue-amylase of Rhizopus delemar to determine the numberaverage molecular weights of the fractions. Good agreement was obtained between the .R. values determined by the kinetic method and those determined by osmotic pressure and reducing end-group measurements.
3. This method is especially useful for the determination of -Mn of linear high polymers having larger -Mn values for which conventional methods would fail to give reliable data. -Mn's over 1, 000, 000 for some amylose fractions could be determined.
The authors wish to acknowledge with gratitude Professor Juichiro Fukumoto and Dr. Yoshio Tsujisaka for their donation of crystalline glut-amylase. We are also greatly indebted to Dr. Takehiko Watanabe for his interest and helpful discussions, and to Messrs. Mutsufumi Kawai and Nobuhiko Okazaki for their technical assistance.View full abstractDownload PDF (818K) -
KOICHI YAGI, YOICHI YAZAWA1966 Volume 60 Issue 4 Pages 450-458
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA subfragment of myosin A [EC 3. 6. 1. 3] was isolated from tryptic digest of HMM by column chromatography on DEAE-cel-lulose. Approximately 40 percent of HMM mass was converted into an enzymatically active, relatively homogeneous component. This process is accompanied by a large change in viscosity from 0.47 to 0.085 dl./g. Sedimentation diagram revealed a relatively high degree of homogeneity and s020, W was 6.2S. The viscosity measurement indicated a low particle assymmetry. Molecular weight of the subfrag-ment was estimated as 1.47×105 from the Scheraga-Mandelkern equation.
No significant difference in properties of ATP and ITP hydrolysis of the subfragment from those of HMM was observed at various pH values. The function of SH-group in the ATPase activity of the subfragment was essentially similar to that of HMM.
The subfragment did not accelerate the polymerization of G-actin, though binding of the subfragment to F-actin was variable from preparation to preparation so far.
We wish to thank Dr. Y. Tonomura for valuable criticisms.View full abstractDownload PDF (1150K) -
MINORU KASUYA, HIDEO TAKASHINA1966 Volume 60 Issue 4 Pages 459-461
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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TADASHI SHIMOJO, KIMIYOSHI OHNO1966 Volume 60 Issue 4 Pages 462-466
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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TADASHI SHIMOJO, KIMIYOSHI OHNO1966 Volume 60 Issue 4 Pages 467-469
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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JIRO TOBARI, TOKUJI KIMURA1966 Volume 60 Issue 4 Pages 470-472
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (197K) -
SUSUMU Y. TAKAHASHI, EIJI OHNISHI1966 Volume 60 Issue 4 Pages 473-475
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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SHUICHIRO KUBO, NAOKAZU KINOSHITA, YUJI TONOMURA1966 Volume 60 Issue 4 Pages 476-479
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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MICHIHIKO TADA, YUJI TONOMURA1966 Volume 60 Issue 4 Pages 480-483
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
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YUTARO HAYASHI, YUJI TONOMURA1966 Volume 60 Issue 4 Pages 484-488
Published: October 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (369K)
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