All issues
Volume 73 (1973)
- Issue 6 Pages 1135-
- Issue 5 Pages 901-
- Issue 4 Pages 683-
- Issue 3 Pages 467-
- Issue 2 Pages 199-
- Issue 1 Pages 1-
Volume 73, Issue 3
Displaying 1-27 of 27 articles from this issue
- |<
- <
- 1
- >
- >|
-
I. Effects of Inhibitors of Nucleic Acid and Protein Synthesis on the Production of Macrophage Migration Inhibitory FactorYasuhiro MIZOGUCHI, Sukeo YAMAMOTO, Seiji MORISAWA1973 Volume 73 Issue 3 Pages 467-474
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSSpecific antigenic stimulation of sensitized lymphocytes leads to the production of macrophage migration inhibitory factor (MIF). Production of MIF is inhibited by mitomycin C, actinomycin D, and puromycin.
The first two of these antibiotics only inhibit MIF production when added to the culture medium at a very early stage of antigenic stimulation.
In contrast, puromycin exerts its inhibitory effect several hours after the antigenic stimulation, but not at an earlier stage. MIF behaves like a protein, so it seems likely that synthesis of RNA is necessary for MIF formation and MIF synthesis may start as early as a few hours after specific antigenic activation of the sensitized lymphocytes. The inhibitory effects of the antibiotics are discussed in relation to the kinetics of MIF production.View full abstractDownload PDF (3667K) -
Masachika IRIE, Fumie SUITO, Terumi SAITO1973 Volume 73 Issue 3 Pages 475-479
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1) Amino acid composition and amino-and carboxyl-terminal amino acids of a ribonuclease (RNase Vs2) having molecular weight of 13, 000 from bovine seminal vesicles were determined.
2) Using antisera against bovine pancreatic RNase A [EC 2.7.7.16] and two RNases from bovine seminal vesicles, RNase Vs1 (major component), and RNase Vs2 (minor component), it was found that two seminal RNases were immunologically indistinguishable but they were distinguishable from bovine pancreatic RNase so far as checked by Ouchterlony's double diffusion test.View full abstractDownload PDF (3420K) -
Takeo MATSUZAWA, Masao NISHIYAMA1973 Volume 73 Issue 3 Pages 481-489
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. By exhaustive photooxidation of rat liver ornithine δ-aminotransferase [EC 2.6.1.13] in the presence of methylene blue, the 22 histidine residues in the native enzyme was decreased to 16 and, the 12 SH groups was decreased to 10 in the photooxidized holo-and apo-enzymes. The inactivation by photooxidation was partially prevented by the presence of α-ketoglutarate but not by ornithine. The semilogarithmic plot of the inactivation was biphasic, indicating two groups involved in this process (the rate constants were 0.5 and 0.12 min-1, respectively).
2. In the native holo-enzyme, 4 SH groups reacted slowly with 5, 5'-dithiobis-(2-nitrobenzoic acid)(DTNB). The blocking of the first 2 SH groups did not change the enzyme activity, but that of the next 2 SH groups brought about 50% inactivation (the rate constant, 0.011 min-1). In the presence of 4M guanidine, 12 SH groups were immediately titrated with DTNB. In the native apoenzyme, by contrast, 10 SH groups were very rapidly titrated with DTNB and three groups were recognized with respect to the rate of reaction with DTNB (the rate constants were 0.50, 0.046, and 0.010 respectively). The blocking of the first 2 SH groups in the apoenzyme brought about simultaneous inactivation to 20% of the control in both enzymatic overall and half reactions. The additions of substrates, ornithine, and α-ketoglutarate, to the apoenzyme showed no effects on the rate of reaction with DTNB.
3. Evidence for a difference in conformation between the holo-and apo-enzymes was obtained by a quantitative micro-complement fixation method. The decrease of antigenic activity in the complement fixation reaction observed with the apoenzyme was recovered to the level of the holo-enzyme by the addition of pyridoxal phosphate. The fact that the apoenzyme treated with 2 equimolar amounts of DTNB was able to bind pyridoxal phosphate was also presented.
4. M odifications of tyrosine, serine, and tryptophan residues were attempted with N-acetylimidazole, diisopropyl fluorophosphate, and 2-hydroxy-5-nitrobenzyl bromide, respectively. Amino groups of the holo-enzyme were modified with acetic anhydride. These modifications did not, however, result in inactivation.View full abstractDownload PDF (1661K) -
XI. Effect of Release of p-Phenylazobenzoyl Residue from p-Phenylazobenzoyl Taka-amylase A on the Enzymatic ActionKaoru OMICHI, Tokuji IKENAKA, Yoshio MATSUSHIMA1973 Volume 73 Issue 3 Pages 491-496
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSp-Phenylazobenzoyl Taka-amylase A (PhAB-TAA) has much less amylase activity and an elevated phenyl maltosidase activity as compared with the intact Takaamylase A (TAA).
When the p-phenylazobenzoylated enzyme (PhAB-TAA) was stored at 0-4°C at pH 6.0 in the dark, a part of p-phenylazobenzoyl residues that had been introduced into Taka-amylase A (TAA)[EC 3. 2. 1. 1] was slowly liberated from the enzyme.
On liberation of the phenylazobenzoyl residue the action pattern of PhAB-TAA gradually changed to that of the intact TAA.View full abstractDownload PDF (936K) -
Keizo WAKU, Yasuo NAKAZAWA1973 Volume 73 Issue 3 Pages 497-504
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. The radioactive precursors, 32Pi, [2-3H] glycerol, and 3H-acetate were injected intravenously into male rabbits and the rates of incorporation into phospholipid fractions of the sarcoplasmic reticulum were estimated.
2. Any distinct differences of specific activities between the phospholipid classes were not observed, although sphingomyelin showed a little lower value than that of other phospholipids.
3. 1-O-Alkyl compounds, especially in ethanolamine phosphoglyceride fraction, got high specific activities even in the early stages of the experiment.
4. The specific activities of 1-O-alkenyl compounds were fairly low as compared with those of 1-acyl and 1-O-alkyl compounds throughout the experiments of 3Hglycerol and 3H-acetate incorporation but reached to the level of 1-acyl compounds in the experiment of 32Pi incorporation. Therefore, it was rather difficult to find the metabolic relationship between plasmalogen and alkyl ether phospholipids.View full abstractDownload PDF (1197K) -
Katsura IZUI1973 Volume 73 Issue 3 Pages 505-513
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSEffects of hydrostatic pressure up to 3, 000 atm on phosphoenolpyruvate (PEP) carboxylase [EC 4. 1. 1. 31] were studied. The enzyme in the absence of its ligands lost some activity by the compression at 1, 000 atm for 15min at 22°C and was inactivated completely by the compression at 2, 000 atm for 15min in complete nonreversibility upon release of pressure. An activation volume for the inactivation was evaluated as about-20ml/mole of the enzyme based on the dependency of inactivation rate on the magnitude of pressure. Investigation of the effect of each ligand on the pressure inactivation of the enzyme revealed the following facts:(i) PEP, one of the substrates, and the allosteric activators such as acetyl-CoA and fructose 1, 6-diphosphate showed no effect (ii) L-Aspartate, one of the allosteric inhibitors, showed a marked protective effect. The extent of protection increased with increasing concentrations of L-aspartate and was saturated at 10mm;(iii) Long chain fatty acid such as laurate, the other allosteric activator, markedly accelerated the pressure inactivation. Discussion is made on the conformational states induced by each ligand based on these results. In addition, the response of enzyme to the effectors at 500 atm where the native subunit structure was possibly retained, was investigated with the intension of getting some information on the change in partial molar volume of the enzyme associated with the allosteric transition. Although no significant pressure effect was observed in this regard, a possible usefulness of this approach is discussed.View full abstractDownload PDF (1581K) -
Yukio NISIMOTO, Jinpei YAMASHITA, Takekazu HORIO1973 Volume 73 Issue 3 Pages 515-521
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSAn antiserum against NADH: hemeprotein oxidoreductase [EC 1. 6. 99. 3] was obtained by injection into rabbits of the enzyme purified from extracts of whole cells of Rhodospirillum rubrum. With the use of the antiserum, the functional role of the enzyme in the electron transport system of chromatophores was studied. The activities for NADH-cytochrome c2 reduction of chromatophores and pure preparations of the enzyme were approximately 50% inhibited in the presence of the antiserum; in the case with the enzyme, approximately 50% of the enzyme formed insoluble complex with the antiserum. With chromatophores, the antiserum inhibited also the activity for succinate-NAD+ reduction driven by either ATP or light and the activity for NADH-induced photosynthetic ATP formation. To the contrary, it did not influence the activity for succinate-cytochrome c2 reduction and the activities for photosynthetic ATP formation induced by ascorbate, succinate, and phenazine methosulfate. On the basis of these findings, it was concluded that the chromatophore membrane contained the same NADH hemeprotein oxidoreductase as the purified enzyme, and that the bound enzyme was functional in donation of electrons from NADH to the photosynthetic, cyclic electron transport system.View full abstractDownload PDF (1199K) -
Yukio NISIMOTO, Jinpei YAMASHITA, Takekazu HORIO1973 Volume 73 Issue 3 Pages 523-528
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSAn antiserum (antiserum-Q) raised against purified NADH: quinone oxidoreductase capable of catalyzing the reduction of 2, 6-dichlorophenol indophenol by NADH was obtained by injecting into rabbits the enzyme purified from whole cells of Rhodospirillum rubrum. When the enzyme was incubated with antiserum-Q, at most approximately half of the activity was inhibited; the inactive complex between the enzyme and the antiserum was insoluble. The activity of chromatophores for reduction of the redox dye by NADH was also inhibited by antiserum-Q; the maximum extent of inhibition was almost the same as that with the purified enzyme. None of the activities of chromatophores for photosynthetic ATP formations induced by ascorbate, succinate, NADH, and phenazine methosulfate, and for reductions of bound cytochrome cc' by succinate and of bound cytochrome B by NADH was influenced by antiserum-Q, whereas the activities for photosynthetic ATP formation induced by NADH and reduction of bound cytochrome B by NADH, but not others, were inhibited by the antiserum against NADH: hemeprotein oxidoreductase (antiserum-H).
The function of NADH quinone oxidoreductase in the electron transport system of chromatophores is discussed.View full abstractDownload PDF (977K) -
Eiichi SOEDA, Takao TORIKATA, Satoru AKUNE1973 Volume 73 Issue 3 Pages 529-536
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSAn enzyme consuming isocitrate was isolated from the adult thorax of the domesticated silkworm, Bombyx mori, and purified 100-fold through the following steps homogenization, butanol treatment, ammonium sulfate fractionation, and Sephadex G-75 gel filtration. The purified preparation, optimally active at pH7.5, was capable of catalyzing conversions among citrate, isocitrate, and cis-aconitate. Hence, this enzyme was identified as an aconitase [citrate (isocitrate) hydro-lyase, EC 4.2.1.3]. Michaelis constants were measured to be 2.70mM for citrate, 0.156mM for isocitrate, and 0.030mM for aconitate. The maximum velocities of conversion were 0.14 for citrate to aconitate and 0.99 for isocitrate to aconitate, relative to a value of 1.0 for the maximum rate of hydration of aconitate.
The crude preparation rapidly lost activity on storage but the purified preparation was more stable. Presence of citrate slightly stabilized the enzyme. Preincubation with ferrous ion and cysteine was not so much effective for the activation.
Most of the aconitase was formed during imaginal molting and found to be included in the subcellular particles obtained from the thoracic muscle by differential centrifugations. From these results, it is concluded that the aconitase is one of the respiratory enzymes in the thoracic sarcosome formed during this stage.View full abstractDownload PDF (1389K) -
Katsuzo NISHIKAWA, Kazuo HOSOI, Junnosuke SUZUKI, Setsuko YOSHIMURA, T ...1973 Volume 73 Issue 3 Pages 537-553
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1) When chromatophores from Rhodospirillum rubrum were illuminated with added [32P] Pi and without added ADP, the radioactive Pi was incorporated into some phosphate compounds. A small but definite amount of the compounds thus formed was adsorbed on charcoal, but not the remainder, most of which was purified and identified with pyrophosphate (PPi).
2) The photosynthetic PPi formation required Me and was stimulated by oligomycin, whereas the photosynthetic ATP formation was stimulated by either Mg2+ or Mn2+ and inhibited by the antibiotic. The photosynthetic PPi formation in the presence of Mg2+ was completely inhibited by Mn2+.
3) Both the photosynthetic PPi and ATP formations were stimulated and depressed by 2, 6-dichlorophenol indophenol plus ascorbate or phenazine methosulfate, but the optimum concentrations of the redox-reagents were different for these two formations.
4) The photosynthetic PPi formation was inhibited by ADP, antimycin A, o-phenanthroline, arsenate, and 2, 4-dinitrophenol but not by ATP. The maximum extent of the inhibition by ADP was approximately 40%.
5) Well-washed chromatophores hydrolyzed PPi into Pi. The pyrophosphatase [EC3. 6. 1. 1] activity was partially depressed in the light even under conditions where the photosynthetic PPi formation did not occur. The activity in darkness was inhibited by Pi and arsenate, but not by ATP or ADP. It was stimulated by 2, 6-dichlorophenolindophenol, 2, 4-dinitrophenol, Li+, Na+, and K+.
6) When chromatophores were depleted of the quinones, the pyrophosphatase activity in darkness decreased partially. When ubiquinone-10 was added, the activity was restored.
7) By sonication of chromatophores, the pyrophosphatase activity in darkness increased to some extent.
8) The mechanism of the photosynthetic PPi formation was discussed with relation to that of the photosynthetic ATP formation.View full abstractDownload PDF (2637K) -
Akio INOUE, Yuji TONOMURA1973 Volume 73 Issue 3 Pages 555-566
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. The rate of rapid change in the UV spectra after adding ATP to H-meromyosin was measured over a range of high concentrations of ATP in 0.2M KCl at pH 7.8 and 3.7°C. The values of Kf and Vf were 0.2mM and 30 sec-1, respectively.
2. The rate of decomposition of the reactive myosin-phosphate-ADP complex, EADPP, was measured using a rapid flow-dialysis method, and the following results were obtained:(i) The rate constants of liberation of radioactive Pi and ADP from EPADP were similar to that of ATPase [EC 3. 6. 1. 3] in the steady state at high ATP concentrations, but were much higher than that of ATPase at low ATP concentrations.(ii) They were unaffected by adding a large amount of non-radioactive ATP.(iii) The rate of liberation of ADP from the simple myosin-ADP complex, which was formed by mixing free enzyme and ADP, was too fast to be the rate-determining step in the ATPase reaction.
3. A typical initial burst occurred both at 0 and 20°C, after adding a large amount of ATP to myosin under conditions, in which all the active sites were occupied by ADP.View full abstractDownload PDF (1889K) -
II. Preparation by Nagarse Digestion and Comparison with Subfragments Prepared by Using Different Proteolytic EnzymesYoichi YAZAWA, Koichi YAGI1973 Volume 73 Issue 3 Pages 567-580
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSAn enzymatically active subfragment of myosin was isolated by Nagarse-digestion of myosin. It was shown to be homogeneous by the determinations of ultracentrifuge, gel filtration of Sephadex G-200 and polyacrylamide-gel electrophoresis. Physical parameters of the subfragment were similar to those of other subfragments prepared by tryptic, chymotryptic, or papain digestion. The subfragment binds strongly to F-actin at the molar ratio of 1, but the activity of actin-activated Mg-ATPase was very low and the acceleration of actin polymerization was hardly observed.
The number of moles of N-terminal amino acids of the subfragment was about 2.62 moles per mole, which suggests an intramolecular peptide bond cleavage. It was also indicated by intrinsic viscosity and gel-filtration chromatography obtained in 5 M guanidine-HCl. In 5 M guanidine-HCl, the subfragment separated into two components and the molecular weight of one component of 32.2 per cent in weight was 4.3×104 and that of another component of 64.8 per cent in weight was about 1.8×104.
The properties were compared with those of the subfragments prepared by using chymotrypsin, trypsin, and trypsin-Nagarse as proteolytic enzymes. Similar results were obtained with the subfragment prepared by tryptic digestion of heavymeromyosin. The extent of proteolysis was less in the one digested by chymotrypsin and more in trypsin-Nagarse than the one digested with Nagarse or trypsin.View full abstractDownload PDF (2257K) -
Masuwo OBINATA, Den'ichi MIZUNO1973 Volume 73 Issue 3 Pages 581-590
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSThe mechanism of λ-phage lysogenization and induction was investigated and the following results were obtained.
1. No strand scission of host DNA was detected by sucrose density gradient centrifugation, but partial denaturation of host DNA during phage lysogenization was detected by a chage in the activity of DNA to bind to a nitro-cellulose membrane.
2. Phage DNA becomes linked covalently with the host chromosome during lysogenization.
3. During lysogenization, early protein of λ-phage is synthesized but late protein is not.
4.λ-Phage DNA, excised during thymine deprivation has no cohesive end, but after thymine supplemention this excised γ-DNA changes, gaining a cohesive end like that of mature phage DNA.View full abstractDownload PDF (1690K) -
Change in DNA-associated Proteins with Concomitant Change in Structure of DNA during Phage InductionMasuwo OBINATA, Den'ichi MIZUNO1973 Volume 73 Issue 3 Pages 591-597
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSThe biological specificity of the structural change of DNA occurring during phage induction was examined in view of the change of the membrane and proteins of E. coli cells occurring at this time.
1. During phage λ induction, the attachment of DNA to the membrane changed. This change was accompanied by the structural alteration of the former as monitored by DNA-binding proteins.
2. Binding specificity of the DNA-binding proteins were examined. The binding proteins isolated from growing E. coli cells were shown to bind specifically to DNA isolated from growing cells, while those isolated from λ-phage induced cells were s pecific to mature phage DNA and the DNA isolated from cells starved of thymine and refed.View full abstractDownload PDF (1024K) -
Katsuyuki SASAKI, Hirohiko KATSUKI1973 Volume 73 Issue 3 Pages 599-608
Published: March 25, 1973
Released on J-STAGE: June 07, 2011
JOURNAL FREE ACCESSA cell-free extract of a soil bacterium, Bacillus sp., which catalyzes the oxidation of C5-branched-chain dicarboxylic acids, such as β-methylmalic and citramalic (CMA) acids without adaptation to these acids, was shown to convert (+) CMA into pyruvate and CoASAc through the following two sequential reactions:
(i)(+) CMA+succiny1-CoA←→(+) CMA-CoA+succinate
(ii)(+) CMA-CoA←→pyruvate+CoASAc
These two reactions seemed to be catalyzed by two enzymes and only reaction (ii) was found to require Mg2+ and to be inhibited by EDTA. However, the two enzymes were not separated from one another by ammonium sulfate fractionation, or by DEAE-Sephadex-, or Sephadex G-200 column chromatography.
The cleavage reaction of (+) CMA was inhibited by various anions, and their inhibitory effects decreased in the order of Hoffmeister's series (SCN->NO3->Cl-> SO22-). Dicarboxylic acids, such as succinic acid and its analogues, monocarboxylic acids, and unsaturated dicarboxylic acids of the cis-form strongly inhibited the activity.
The (+) CMA-CoA lyase reaction seems to be reversible because partially purified (+) CMA-cleavage enzymes catalyzed formation of radioactive CMA from 14CCoASAc and pyruvate and because the 14C-CMA formed was dextrorotatory.
The enzymes concerned were demonstrated in cells grown on various organic acids, and so seemed to be constitutive enzymes, unlike those in Pseudomonas.View full abstractDownload PDF (1657K) -
I.Solubilization and Stability of Lubrol ExtractsToshiko NAKAO, Makoto NAKAO, Nobuko MIZUNO, Yoshiko KOMATSU, Michiya F ...1973 Volume 73 Issue 3 Pages 609-619
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSTo purify Na, K-ATPase [EC 3. 6. 1. 3], its solubilization with Lubrol was examined. Pretreatment of the enzyme with a high concentration of NaI was also examined in detail. Ouabain-insensitive ATPare was almost completely removed by the latter procedure. Fiske and SubbaRow's method was slightly modified for the determination of phosphate in the presence of Lubrol.
The inhibition of the ATPase by Lubrol and the time course of loss of activity in Lubrol extracts were studied. Pretreatment of Lubrol with a mixed resin increased its effectiveness for extraction and reduced its inhibitory effect on activity. The inhibitory effect of ouabain was apparently decreased by Lubrol, but restored by addition of heat-treated microsomes. The effective factor in the microsomes may be a lipid fraction. Conditions for efficient extraction of the enzyme with Lubrol were examined. Extraction was best in the absence of salt and ATP, using resintreated Lubrol. The supernantant fraction obtained by centrifugation of the Lubrol extract at 160, 000×g for 60 min showed higher specific activity than that reported previously for soluble enzymes. It also showed higher sensitivity to ouabain (2×10-5M ouabain caused complete inhibition) and slightly higher stability.
The extract was eluted as a single, symmetrical peak from a Sepharose 6B column, with an apparent molecular weight of 500, 000. From the elution profile the preparation seemed to be homogeneous, but the time course of the reaction suggested the existence of at least two active components.View full abstractDownload PDF (1814K) -
Masao TAKEDA, Yûzo OHGA1973 Volume 73 Issue 3 Pages 621-629
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSA single intraperitoneal injection of glucagon to rat leads, within 5 min, to a 30-fold increase in the concentration of adenosine 3', 5'-monophosphate (cyclic AMP) in liver. The high level of cyclic AMP drops rapidly, returning to the original level after 90 min. Induction of liver tyrosine aminotransferase [EC 2. 6. 1. 5] occurs at 30 min following administration of the hormone and the high level of enzyme activity remains for 2 hr and then gradually decreases. During the enzyme induction, lysinerich (F1) histone among nuclear proteins is only a detectable protein whose phosphorylation is significantly stimulated. Kinetic studies indicate that the phosphorylation of a specific site of histone F1 precedes the induction of tyrosine aminotransferase, and that the rate of this phosphorylation is proportional to the intracellular cyclic AMP concentration. Protein kinase [EC 2. 7. 1. 37] activity, which is measured in vitro without adding cyclic AMP, increases at 5 min and returns to the control level at 75 min. Tryptic phosphopeptides obtained from histone F1 preparations, which are phosphorylated in vivo and in vitro, are electrophoretically identical. These results confirm that histone F1 serves as a substrate in vivo for cyclic AMP-dependent protein kinase.View full abstractDownload PDF (3766K) -
I.Preparation of p-Nitrophenyl 2-Acylamino-2-deoxy-β-D-glucopyranosides and Their Susceptibility toward Enzymatic HydrolysisKazuhiko YAMAMOTO1973 Volume 73 Issue 3 Pages 631-635
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSIn order to investigate the N-acyl specificity of Taka-N-acetyl-β-D-glucosaminidase [EC 3. 2. 1.30], some of p-nitrophenyl 2-acylamino-2-deoxy-β-D-glucopyranosides containing formyl, propionyl, n-butyryl, isobutyryl, and benzoyl groups as N-substituent were synthesized.
The substrate analogs other than N-benzoyl derivative were hydrolysed by this enzyme. Thus, the N-acyl specificity of this enzyme was not restricted to N-acetyl group, although it was found to be the most favorable substituent for the enzymatic reaction. The specificity was suggested to be controlled by the steric factor of the substrate N-substituent. In addition, other factors such as a hydrophobic and an electronic factors are also presumed to be concerned.
It was confirmed by the enzymic reaction and melting point determination that O-N acetyl migration in N-acylation process did not occur.View full abstractDownload PDF (683K) -
IV. The Nature of the Kinetically Inactive Complex of Cytochrome Oxidase with CyanideShinya YOSHIKAWA, Yutaka ORII1973 Volume 73 Issue 3 Pages 637-645
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSInhibition by cyanide of cytochrome oxidase [EC 1. 9. 3. 1] occurs at cyanide concentrations far below those required for the complex formation with either the reduced or oxidized form. Such a discrepancy was shown to be due to the fact that a kinetically inactive complex is formed between cyanide and an intermediate state of cytochrome a, which was different spectrally from either static species, the reduced and oxidized cytochrome. The nature of the intermediate form was suggested to be the oxygenated form, although a possible involvement of another type of ferricytochrome a could not be ruled out.
The present investigations also yielded the titration data of cytochrome awith cyanide which indicate that about one half of the heme a is catalytically active with respect to the reaction with molecular oxygen.View full abstractDownload PDF (1564K) -
II. Crystallization and Chemical Properties of EndonucleaseIkuo SUHARA, Masahiko YONEDA1973 Volume 73 Issue 3 Pages 647-654
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. The endonuclease from Acrocylindriu purified about 60-fold by means of CM-cellulose and hydroxyapatite column chromatography. This enzyme preparation was free from exonuclease, ribonuclease [ribonucleate guaninenucleotido-2'-transferase (cyclizing), EC 2. 7. 7. 26, or ribonucleate nucleotido-2'-transferase (cyclizing), EC 2. 7. 7. 17], phosphodiesterase [orthophosphoric diester phosphohydrolase, EC 3. 1. 4. 1], phosphomonoesterase [orthophosphoric monoester phosphohydrolase, EC 3. 1.3. 1 or 3. 1. 3. 2], and protease.
2. Furthermore, the endonuclease was obtained as needle crystals. The crystalline endonuclease showed a single peak with the sedimentation constant of 2.5 S in an ultracentrifuge.
3. The molecular weight of the crystalline endonuclease was estimated to be 19, 000-21, 000.
4. It was demonstrated by amino acid analysis that the tryptophan content in the endonuclease was higher than that in Staphylococcal nuclease (1).
5. The N-terminal amino acid of the enzyme was determined as asparagine or aspartic acid.
6. The isoelectric point of the enzyme was pH 6.8.View full abstractDownload PDF (7005K) -
Kazuko SHIBATA-SEKIYA1973 Volume 73 Issue 3 Pages 655-658
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (536K) -
Hidekazu IWASAKI, Teruo MATSUBARA1973 Volume 73 Issue 3 Pages 659-661
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (392K) -
II. Gas Chromatographic Quantitation of Methyl GlycosidesSusumu ANDO, Toshio ARIGA, Tamio YAMAKAWA1973 Volume 73 Issue 3 Pages 663-665
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (446K) -
Kenji DOI, Akemi DOI, Takeshi OZAKI, Toshio FUKUI1973 Volume 73 Issue 3 Pages 667-670
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (2254K) -
Chia Lien LIU, Kozo OHTSUKI, Hiroyuki HATANO1973 Volume 73 Issue 3 Pages 671-673
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (426K) -
Kenji TAKAHASHI, Wen-Jong CHANG1973 Volume 73 Issue 3 Pages 675-677
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (404K) -
Masataka YOSHINO, Yasuhiko KAWAMURA, Nobuaki OGASAWARA1973 Volume 73 Issue 3 Pages 679-682
Published: March 25, 1973
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (527K)
- |<
- <
- 1
- >
- >|