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Volume 46 (1959)
- Issue 6 Pages 669-
- Issue 5 Pages 535-
- Issue 4 Pages 397-
- Issue 3 Pages 219-
- Issue 2 Pages 107-
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Volume 46, Issue 3
Displaying 1-19 of 19 articles from this issue
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MITSUO NISHIMURA1959 Volume 46 Issue 3 Pages 219-223
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFrom the green cells of Euglena, the isolation was carried out for a new cytochrome having a prosthetic group similar to that of the mammalian cytochrome c. Characteristic of this cytochrome are its high oxidation-reduction potential (E0'=0.36 v.) and its close association with photosynthetic apparatus. The chlorophyll-less cells produced either by prolonged hetero-trophic dark culture or by mutation induced by streptomycin- or heat-treatment contain no trace of the cytochrome. The new cytochrome, which seems to play some role in the mechanism of photosynthesis of the green Euglena, was tentatively named Euglena-cytochrome-552.
The author expresses many thanks to Prof. H. Tamiya and Prof. A. Takamiya for their kind guidance and valuable criticism. He is also indebted to Prof. H. Huzisige for his suggestions. This work was supported in part by a research grant from the Ministry of Education.View full abstractDownload PDF (199K) -
MITSUO NISHIMURA, HIROSI HUZISIGE1959 Volume 46 Issue 3 Pages 225-234
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The Euglena cells synthesize chlorophylls a and b in the light. In the dark, chlorophylls are not formed, and protochlorophyll is detected in a very small amount. The protochlorophyll present in the white cells was extracted and identified.
2. The photochemical transformation of protochlorophyll to chlorophyll a was shown to occur in the dark-grown cells in the initial stage of illumination.
3. After the illumination was started, the actual increase in chlorophyll content occurred following a lag period of about 15 hours.
4. The rate of chlorophyll formation in the non-proliferating suspensions of Euglena depends on the wavelength of the illumination. The action spectrum of chlorophyll formation has two peaks; one lies about 650mμ, the other in the violet region of the spectrum. Chlorophyll is inferred to be the principal photosensitizer in the later period of chlorophyll formation.
The authors wish to express their gratitude to Prof. H. Tamiya for kind guidance in this work. They are also indebted to Prof. A. Takamiya for his valuable suggestions.View full abstractDownload PDF (402K) -
I. ACTION OF CARBOXYPEPTIDASE ON MONO-, DI-, TRI-, TETRA- AND PENTA-GLYCYL-L-TYROSINENOBUO IZUMIYA, HAKARU UCHIO1959 Volume 46 Issue 3 Pages 235-245
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A number of the peptides Glyn-L-Tyr in which n are 1, 2, 3, 4 and 5 have been synthesized and tested as substrates for carboxypeptidase.
2. By the use of Gly2-L-Tyr, the pH optimum of hydrolysis was found to be near 8.5. For comparison, the pH optimum for CbzGly-L-Tyr was checked and found to be near 7.6.
3. The values of proteolytic coefficients at the initial substrate con-centrations of 0.025M, 0.015M, 0.01M and 0.005M, and Cmax, determined at 30° and in Tris buffer at pH 8.5, were taken as measures of the relative susceptibility of hydrolysis of the substrates by carboxypeptidase. Chroma-tographic analysis of the reaction mixture proved the simple hydrolysis of the substrates to L-tyrosine and corresponding polyglycine Glya (n=1_??_5).
4. The same hydrolytic rates by carboxypeptidase of the substrates Glyn-L-Tyr (n=2_??_5) were observed; the Cmax of the substrates were 16_??_17. Gly-L-Tyr was hydrolyzed approximately 1/200 times slowly than Glyn-L-Tyr (n=2_??_5).
The authors wish to thank Prof. S. Shibuya for his interest, and Dr. A. Tanaka for his discussion in this study.View full abstractDownload PDF (452K) -
NIKICHI OKUMURA, SABURO OTSUKI, HIROYUKI NASU1959 Volume 46 Issue 3 Pages 247-252
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The present study has been undertaken to determine, as the first step, the pattern of free amino acids and related compounds in the brain of the normal rat. Secondarily, the changes of the pattern due to fasting, insulin hypoglycaemic coma, repeated electroshocks, and administration of chlorpromazine or β-phenylisopropylmethylamine have been studied by chromatography on Dowex 50-×4 columns.
2. During insulin hypoglycaemic coma, free aspartic acid concentration considerably increased, while free glutamic acid and alanine concentrations decreased. Both the fall of glycerophosphoethanolamine and the rise of threonine taking place in this treatment were also found in fasting rat.
3. In the irritable stage produced by repeated electroshocks, the glutamic acid content slightly increased without any change in other constituents.
4. Repeated injection of chlorpromazine for 30-60 days increased glutamic acid, aspartic acid, γ-aminobutyric acid and taurine content, besides a decrease of glycerophosphoethanolamine.
5. Repeated injection of β-phenylisopropylmethylamine produced no marked changes in the pattern, but only the increase of N-acetylaspartic acid concentration was observed.View full abstractDownload PDF (275K) -
KAZUKO FUJITA1959 Volume 46 Issue 3 Pages 253-268
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The process of oxidative assimilation in the green alga, Chlorella ellipsoidea, was investigated, using methyl- and carboxyl-labelled acetic acids and glucose as the substrates.
2. It was found that the rate as well as the balance sheet of the oxidative assimilation of carboxyl carbon of acetic acid was subject to considerable change in the course of cellular life-cycle of the organism. No significant change with this respect was observed with methyl carbon as the substrate.
3. The efficiency of acetic acid incorporation was found to be very high, in the most favorable cases, 1.6 atoms carbon being assimilated per one molecule acetic acid consumed.
4. The conversion of the methyl and carboxyl carbon of acetic acid was investigated by isotope experiments. The methyl carbon was found to be converted exclusively into cell material; while two-thirds of the carboxyl carbon was found to be incorporated in cell material. The remaining one-third of the carboxyl carbon was discharged as carbon dioxide.
5. The incorporation of the carboxyl carbon was inhibited by cyanide, and according to the first order sygmoid curve (see text); 50 per cent inhibition being reached at 10-4.0M potassium cyanide; the incorporation from the methyl carbon and C14O2 evolution from the carboxyl carbon were found to be more refractory to the poison, 50 per cent inhibition being reached at 10-3.0M of potassium cyanide. No complete inhibition of the incorporation of methyl carbon and the C14O2-evolution from carboxyl carbon was observed at a concentration of potassium cyanide as high as 10-2M.
6. Carbon dioxide (unlabelled) was found to inhibit all the metabolic processes in accord with the first order sygmoid curve; partial pressure of carbon dioxide for 50 per cent inhibition of the incorporation from the carboxyl, and from the methyl carbon, and CO2 evolution from the carboxyl and methyl carbon were found to be 10-1.5, 10-1.0, 10-1.0, 10-1.0 atom, respectively.
7. 2, 4-dinitrophenol was found to inhibit the incorporation of carboxyl carbon into the organism.
I wish to express my thanks to Prof. H. Tamiya for suggesting this investigation as well as for constant guidance in the course of the work. Thanks are also due to Prof. A. Takamiya for some valuable suggestions.View full abstractDownload PDF (593K) -
SATOSHI SASAKI1959 Volume 46 Issue 3 Pages 269-279
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The tooth germs of the dog 1 or 2 months after birth were separated into three tissue parts: The enamel pulp including the dental sac, the dental papilla and the calcified part, the their respiratory activities were determined by the Warburg manometric technique. The mean Qo2 values were 2.63±0.76 for the enamel pulp including the dental sac part, 3.56±1.07 for the dental papilla and for the calcified part an accurate value could not be determined, although respiration was always observed. The question as to what kind of cell component was responsible for the respiration of the calcified part could not be clarified even by means of histological research.
2. α-Ketoglutarate had the effect of increasing O2-uptake in all three tissue parts. Other substrates: glucose, lactate, pyruvate, citrate, succinate, fumarate, malate, and glutamate had no effect.
3. Methylene blue (3×10-4M) and cytochrome c (6×10-4M) increased O2-uptake in all three parts.
4. Removing the calcium ion from the medium had no effect on the rate of endogeneous respiration of the tissues.
5. From the results of the correlation in respiration to the degree of calcification, it was suggested that the maximum respiratory activity for each tissue part occurs at different stages of germ development.
6. The RQ value was about 1.0 for dental papilla, and for the enamel pulp including the dental sac part, a definite value was not obtained but was supposed to be smaller than that for dental papilla.
A Scientific Research Grant from the Ministry of Education provided part of the funds for this work.View full abstractDownload PDF (459K) -
A METHOD FOR PREPARING THE FOURTH COMPONENT OF COMPLEMENTSHOJIRO SATO, HIROSHI FUNAKOSHI1959 Volume 46 Issue 3 Pages 281-292
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The effect of metaperiodate on guinea pig complement activity was investigated quantitatively.
2. Metaperiodate destroys strongly a hemolytic system and a factor of which responsible for this destruction is complement. This action of metaperiodate is greatly reduced by ethylene glycol. The latter does not affect a hemolytic system appreciably.
3. The first, second and third complement components (C1', C2' andC3') are easily destroyed by metaperiodate, but the fourth component (C4') is fairly resistant to the reagent.
4. The best procedure for preparing a preparation of C4' is to treat two volumes of 1:3 diluted serum with one volume of 0.02M NaIO4 for 30 to 60 minutes at room temperature and then to neutralize the excess of reagent with ethylene glycol. The activity of this preparation combined with an equal volume of ammonia-treated serum, concentrations of both preparations being 1:8 dilution in terms of original serum, was equivalent to that of 1:38 diluted serum, that is, about one fifth.
5. The mode of action of metaperiodate on complement activity was discussed.View full abstractDownload PDF (580K) -
II. SULFATE FORMATION FROM L-CYSTINE BY MOLDSYATARO OBATA, YOSHINORI ISHIKAWA1959 Volume 46 Issue 3 Pages 293-295
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSulfate formation by 19 strains of molds in L-cystine media in which L-cystine was the sole nitrogen source was compared. Except Penicillium digitatum and Oospora lactis, all of the strains belonging to the genera Scopu-lariopsis, Penicillium, Paecilomyces, Alternaria, Botrytis, Cladosporium, Monascus, Oospora, Fusarium, Monilia, and Aspergillus formed sulfate from L-cystine. Aspergillus niger showed the highest ability of the sulfate production.
The authors wish to express their thanks to Dr. Y. Sasaki of the Institute of Ap-plied Mycology, Hokkaido University, for his kindly supplying microorganisms used in this study.View full abstractDownload PDF (120K) -
II. PHENYLAZOBENZOYLATION OF TAKA-AMYLASE ATOKUJI IKENAKA1959 Volume 46 Issue 3 Pages 297-304
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. p-Phenylazobenzoyl chloride was reacted with Taka-amylase A at various pH. By the phenylazobenzoylation at pH 6.0, the decrease of amylase activity was associated with the introduction of PhAB-residue. The amylase activity was almost lost by the introduction of about one mole of PhAB residue.
2. The changes of enzymatic activities toward α-phenylmaltoside, p-nitrophenyl-α-maltoside and maltotetraose during phenylazobenzoylation was measured at pH 6.0. It was found that α-phenylmaltosidase activity of Taka-amylase A increases about 2.5 fold over the original activity. While the enzymatic activity to hydrolyze p-nitrophenyl-α-maltoside and maltote-traose suffers only a slight change by the treatment.
3. It was suggested that the site of combination of the PhAB residue seems to be a ε-amino group of the special lysine residue situated in the vicinity of the active site.
The author wishes to express his gratitude to Prof. S. Akabori for his kind guidance throughout the investigation and to Mr. T. Usami and Mr. Y. Imai for their technical assistance. The author also wishes to thank the Sankyo Co. Ltd. for their kind supply of “Takadiastase Sankyo” and Mr. M. Nomofo for his kind supply of the protease obtained from Streplomyces griseus.View full abstractDownload PDF (331K) -
TAIICHE NIHEI, YUJI TONOMURA1959 Volume 46 Issue 3 Pages 305-319
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The effects of divalent cations on myosin B-NTPase activity depend primarily on their ionic radii (r). The v-r curve assumes a bell-shaped form, having its maximum at 0.95 and 0.9 A for ATPase and ITPase, respec-tively. At low ionic strength the v-r curve is less steep than the one at high ionic strength.
2. Kinetic analysis of the effect of Ca++ leads us to the conclusion that Ca++ activates ATPase by its complex-formation with ATP.
3. From the pH dependence of Km, it is concluded that ATP4- is the true substrate of ATPase.
4. The temperature coefficients of Vm and Km of ATPase are measured at a wide range of temperature. The log Vm-1/T relation is found to bend at about 0°.
5. When the concentration of ATP becomes higher than 1mM, ATPase is inhibited, while, at still higher concentrations of ATP (>6mM), activation of ATPase takes place.
6. EDTA and PCMB increases Vm and Km of ATPase, and simultaneous-ly they eliminate the substrate-inhibition and -activation.
7. The pH-activity curves of ATPase in the presence of EDTA and of high concentrations of ATP does not show the depression at neutral pH, which is one of the characteristics of the myosin-ATPase under ordinary conditions.
8. ITPase is scarecely activated by PCMB and its pH-activity curve lacks the depression at neutral pH.
9. Based on these results, a mechanism is proposed for the interaction between NTP and myosin B. This mechanism gives satisfactory explanations not only for the observations reported here but also for various other phenomena observed thus far with the myosin B-NTP system.
We wish particularly to thank Prof. J. Horiuti (Research Inst. for Catalysis) and Prof. H. Tamiya (Tokyo Univ.) for their support and encouragement in carrying out this work; Dr. S. Watanabe (Chemistry Dept.) for his advice in writing this paper in English. This study has been aided in part by a grant in aid for Fundamental Scientific Research of the Ministry of Education given to the Research Group on the ‘Mechanism of Enzyme Action’.View full abstractDownload PDF (623K) -
V. CRYSTALLIZATION OF CYTOCHROME C FROM WHEAT GERMBUNJI HAGIHARA, KUNIO TAGAWA, ICHIRO MORIKAWA, MASATERU SHIN, KAZUO OK ...1959 Volume 46 Issue 3 Pages 321-327
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSWheat germ was treated with ethylacetate and cytochrome c was ex-tracted from it with 30 per cent saturated ammonium sulfate. It was then fractionated with AS. The precipitate between 75-95 per cent saturation was dialyzed, adsorbed on Amberlite XE-64, and eluted with 0.3N NH+ buffer of pH 7 after washing the column with 0.1N buffer. The adsorp-tion, washing and elution treatments were repeated, and then the cytochrome c was chromatographed first in the oxidized and then in the reduced state. The purified cytochrome c was then easily crystallized in a similar way to mammalian cytochrome c into long plates. The yield was about 3μmoles per 10kg. germ.View full abstractDownload PDF (636K) -
TSURU WADA1959 Volume 46 Issue 3 Pages 329-336
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Antisera against Taka-α-amylase were produced in rabbits by the injection of crystalline Taka-α-amylase.
2. Serological properties of antisera obtained were studied and it became clear that the antisera contain only a single homogeneous antibody with a moderate high activity.
3. The inhibition of Taka-amylase activity by antibody, and the in-hibitory effect of starch and other carbohydrates on the amylase-antiamylase reaction, were clearly demonstrated.
4. The effect of an anti-Taka-amylase antibody on the various amylases of other origins was studied. It was found that anti-Taka-amylase antiserum inhibits the α-amylase activities of Aspergillus usami, awamori and sojae; on the other hand the α-amylase activities of other molds and β-amylase activities of all strains tested were unaffected.
5. Heat denatured Taka-amylase did not inhibit the reaction between the Taka-amylase and its antiserum.
The author is indebted to Prof. S. Akabori for his encouragement and guidance, and to Prof. T. Ogata, in whose laboratory the immunization experiment was perfomed, for his helpful advices and suggestions, especially on the immunological technique. The author also wishes to thank Akabori laboratory, University of Osaka, for generous supply of crystalline Taka-α-amylase and to Dr. Ando for his kind gifts of mold α-amylase preparations.View full abstractDownload PDF (1057K) -
II. ACTION OF α-CHYMOTRYPSIN ON AMINOACYL-L-TYROSINE ETHYL ESTERSNOBUO IZUMIYA, TAKESHI YAMASHITA1959 Volume 46 Issue 3 Pages 337-345
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A number of aminoacyl-L-tyrosine ethyl ester hydrochlorides have been synthesized and tested as substrates for α-chymotrypsin.
2. The stability of aminoacyltyrosine esters, in which the aminoacyl substituents are glycyl, L-alanyl, L-α-aminobutyroyl, L-norvalyl, L-norleucyl, L-valyl, L-leucyl, β-alanyl and ε-norleucyl groups, was tested in the absence of the enzyme at pH 8.0.
3. The pH optimum of chymotrypsin activity for glycyltyrosine ethyl ester was found to be near 8.3.
4. The enzyme catalyzes at least two reactions: hydrolysis of the ester linkage to form the corresponding dipeptide and formation of the ninhydrin negative product. β-Alanyl and ε-norleucyl tyrosine esters, however, are simply hydrolyzed, yielding no ninhydrin negative products.
5. The rates of action of the enzyme was decreased markedly by the presence of large side chain groups in the N-terminal L-amino acid residues of the substrates.View full abstractDownload PDF (368K) -
SHINJI ISHIKAWA1959 Volume 46 Issue 3 Pages 347-359
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDPN-L-Gulonic dehydrogenase was purified from guinea pig liver and its properties were described.
1. The enzyme was purified about 20 fold using ammonium sulfate fractionation and negative adsorption with DEAE-cellulose.
2. The purified enzyme was separated from TPN-L-gulonic dehy-drogenase, sorbitol dehydrogenase, and gulonolactonase, but dehydrogenation reaction could not be separated from decarboxylation reaction.
3. L-Xu was identified as the reaction product.
4. The reverse reaction was not demonstrated.
5. Some properties of the enzyme were discussed compared to other β-dehydrogenation-decarboxylation enzymes.
The author wishes to thank Dr. N. Shimazono for his continuous interest and advice during the course of this investigation, and is grateful to Miss K. Noguchi for her skillful technical assistance. The author is also indebated to Drs. H. Masamune of Tohoku University, Y. Takagi of Osaka University, T. Nakajima of Pharmaceutical Department of Tokyo University, S. Nasuno of Institute of Applied Microbiology of Tokyo University for their kind supply of some of the materials used in this work. This work was supported in part by a grant for scientific research'from the Ministry of Education.View full abstractDownload PDF (538K) -
KAZUO YAMADA1959 Volume 46 Issue 3 Pages 361-372
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A presence of two types of lactonase in the cell fractions of animal tissues has been demonstrated. They were tentatively named Lactonase-I and -II for soluble and microsomal fraction, respectively.
2. Lactonase-I has been purified 21-fold from acetone powder. It re-quired divalent cations such as Mg++ and Mn++ for activation. It has also been shown to have optimum pH 6.8-7.0.
3. Lactonase-I has been shown to have a rather broad substrate specificity and to act on L-gulonolactone, D-glucuronolactone and other lactones, whereas Lactonase-II was specific to glucuronolactone.
4. Lactonase-I has been proved to be an SH-enzyme. Michaelis constant has been determined. Lactonase has been found in the liver of a rat but not in the kidneys, brain, lung, spleen, or heart.
5. The significance of this enzyme in the L-ascorbic acid biosynthesis has been discussed.
The writer's thanks are due to Prof. N. Shimazono and Dr. S. Ishikawa and the other members of this laboratory for their kind guidance and assistance, and to Dr. H. S. Isbell and Dr. T. Nakazima who kindly donated part of the substrates.View full abstractDownload PDF (489K) -
SHÔJI MIZUSHIMA, MICHIKO NAKANO, KIN-ICHIRÔ SAKAGUCHI1959 Volume 46 Issue 3 Pages 373-381
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Aerobacter cloacae isolated from soil was found to show a cyanide-insen-sitive growth adaptively.
2. The glucose oxidation by cyanide adapted cells was cyanide insensi-tive, whereas that by cyanide non-adapted cells was remarkably inhibited by cyanide.
3. The oxidation of DPNH and succinate by the cell-free extract pre-pared from both cyanide adapted and cyanide non-adapted cells, was cyanide insensitive. Almost all of the oxidase activity was localized in the particulate fraction.
4. A cytochrome component which has absorption maxima at 557 and 530mμ was detected in particulate fraction and was found to be reduced by the addition of DPNH, succinate and dithionite.
5. The physiological significance of this cyanide insensitive terminal oxidase system was discussed.
The authors wish to express their sincere appreciation to Mr. K. Komagata, The Institute of Applied Microbiology, University of Tokyo, for his kind advise in the diagnosis of bacteria.View full abstractDownload PDF (340K) -
MITUO EBATA1959 Volume 46 Issue 3 Pages 383-390
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSLinear poly-ε-aminocaproyl-DL-alanine and poly-ε-aminocaproyl-L-alanine could be partly hydrolysed by the action of crystalline trypsin. Considerable decrease of specific viscosity of the reaction mixture occurred though total amounts of the hydrolysis were relatively small. Optimum concentrations of hydrogen ion in the reaction mixture were 7.1-7.4. These polymers make resistance to the action of high concentrations of α-chymotrypsin and car-boxypeptidase. Two temperature optima were found at 30° and 60°.
The author wishes to express his hearty thanks to Prof. F. Egami of Nagoya Uni-versity, J. Noguchi of this university, Dr. R. Sato, Osaka University and to Dr. N. Sakota, Dainippon Zoki Laboratory, for their kind encouragements throughout the course of this work. The author is also grateful to Miss K. Matsunag a for her technical assistances.View full abstractDownload PDF (315K) -
TAKASHI YUSA1959 Volume 46 Issue 3 Pages 391-393
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (531K) -
TAKASHI KUSAKA1959 Volume 46 Issue 3 Pages 395-396
Published: March 25, 1959
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (68K)
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