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Masayoshi TAKAKUWA, Yasuo WATANABE
1981 Volume 45 Issue 10 Pages
2167-2173
Published: 1981
Released on J-STAGE: March 27, 2006
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Variations in lipid components of washings and homogenate of pressed baker's yeast were investigated during the storage of pressed baker's yeast at 30°C . Washings represents the substances which had leaked out from cells. Homogenate represents those contained in whole cells. Lipids in yeast washings increased toward softening, the phospholipids in yeast homogenate decreased continuously during storage. Two stages, an earlier period of storage (Stage I) and a later period of storage (Stage II) were observed in the degradation of phospholipids. Free fatty acid which was the main degradation product of phospholipid accumulated in Stage II, particularly at softening. The order in phospholipid degradation was PC>PE>PI+PS (PI>PS). Moreover, when washings of stored yeast at softening were assayed using
14C-acyl PC, the release of
14C-acyl fatty acid was observed.
These results suggest that phospholipids were degraded by some phospholipid-deacylating enzymes toward softening. From the results of lipid analysis, we inferred that the responsible enzymes were phospholipases.
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Yohei NATORI, Tomohisa NAGASAKI
1981 Volume 45 Issue 10 Pages
2175-2182
Published: 1981
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Mutation of
Pseudomonas N842 was carried out to increase CoQ
10 production. The productivity of CoQ
10 was improved considerably by repeated mutation, and the content of CoQ
10 per unit cell of the fifth generation mutant was approximately 6 times that of the wild strain,
Pseudomonas N842. CoQ
11, which was hardly detectable in the wild strain, increased significantly by mutation, and the ratio of CoQ
11 to total CoQ exceeded 20 % in the fourth generation mutant. Intermittent feeding of glucose to the culture medium during cultivation increased cell yield and CoQ production. When total glucose added was 5 times that of basal medium, cell yield and CoQ formation respectively increased about 3 and 4 times.
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Kazuo YOSHIOKA, Naoki HASHIMOTO
1981 Volume 45 Issue 10 Pages
2183-2190
Published: 1981
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Alcohol acetyltransferase responsible for the formation of acetate esters during beer fermentation was found to be localized at the cell membrane of brewers' yeast. This cell membrane-bound enzyme was purified 120-fold by solubilization with Triton X-100, gel filtration on a Sepharose 6B column and chromatography on a DEAE-Sephadex A-50 column. The enzyme was most active at 30°C at pH 78. It was least active against C
3 alcohol among C
1C
6 alcohols, and slightly more active against straight-chain alcohols than against branched-chain alcohols with the same carbon number. The enzyme was strongly inhibited by unsaturated fatty acids, heavy metal ions and sulfhydryl reagents.
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Takashi SAKAGUCHI, Takao HORIKOSHI, Akira NAKAJIMA
1981 Volume 45 Issue 10 Pages
2191-2195
Published: 1981
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The adsorption of uranium by chitin phosphate and chitosan phosphate was investigated to obtain information on uranium recovery from aqueous systems, especially sea water and uranium mine waste water. The adsorption of uranium by chitin phosphate and chitosan phosphate was much greater than copper, cadmium, manganese, zinc, cobalt, nickel, magnesium and calcium. The adsorption of uranium was very rapid during the first 10 min and was affected by pH of the solution, temperature, granule radius and the co-existence of carbonate ion. The amounts of uranium adsorbed on the adsorbents increased linearly as the external uranium concentration increased. Uranium adsorbed on chitin phosphate easily desorbed with diluted sodium carbonate solution. On the other hand, uranyl and cobalt ions were separated from each other by using chitin phosphate.
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Isamu SHIIO, Shin-ichi SUGIMOTO
1981 Volume 45 Issue 10 Pages
2197-2207
Published: 1981
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In the biosynthetic pathway of aromatic amino acids of
Brevibacterium flavum, ratios of each biosynthetic flow at the chorismate branch point were calculated from the reaction velocities of anthranilate synthetase for tryptophan and chorismate mutase for phenylalanine and tyrosine at steady state concentrations of chorismate. When these aromatic amino acids were absent, the ratio was 61, showing an extremely preferential synthesis of tryptophan. The presence of tryptophan at 0.01 mM decreased the ratio to 0.07, showing a diversion of the preferential synthesis to phenylalanine and tyrosine. Complete recovery by glutamate of the ability to synthesize the Millon-positive substance in dialyzed cell extracts confirmed that tyrosine was synthesized
via pretyrosine in this organism. Partially purified prephenate aminotransferase, the first enzyme in the tyrosine-specific branch, had a pH optimum of 8.0 and
Km's of 0.45 and 22 mM for prephenate and glutamate, respectively, and its activity was increased 1 5-fold by pyridoxal-5-phosphate. Neither its activity nor its synthesis was affected at all by the presence of the end product tyrosine or other aromatic amino acids. The ratio of each biosynthetic flow for tyrosine and phenylalanine at the prephenate branch point was calculated from the kinetic equations of prephenate aminotransferase and prephenate dehydratase, the first enzyme in the phenylalanine-specific branch. It showed that tyrosine was synthesized in preference to phenylalanine when phenylalanine and tyrosine were absent. Furthermore, this preferential synthesis was diverted to a balanced synthesis of phenylalanine and tyrosine through activation of prephenate dehydratase by the tyrosine thus synthesized. The feedback inhibition of prephenate dehydratase by phenylalanine was proposed to play a role in maintaining a balanced synthesis when supply of prephenate was decreased by feedback inhibition of 3-deoxy-D-
arabino-heptulosonate 7-phosphate (DAHP*) synthetase, the common key enzyme. Overproduction of the end products in various regulatory mutants was also explained by these results.
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Kunihiko GEKKO, Ichiro SATAKE
1981 Volume 45 Issue 10 Pages
2209-2217
Published: 1981
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The amount of unfreezable water in lysozyme and bovine serum albumin in aqueous solutions of xylitol, sorbitol, glucose and sucrose was estimated by a differential scanning calorimeter according to new analytical methods. The antemelting point of aqueous polyol solutions seemed to shift to a higher temperature upon addition of protein, but the incipient melting point was not affected by the coexisting protein. The amount of unfreezable water in both proteins, as well as the heat of fusion of ice, decreased with increasing polyol concentration, regardless of the kind of polyols added. On the basis of these results, the solvation structure of the protein in these three-component systems and the mechanism of the polyol-induced stabilization of protein were discussed assuming protein-polyol interactions.
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Yukio FURUICHI, Takao TAKAHASHI
1981 Volume 45 Issue 10 Pages
2219-2224
Published: 1981
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The present study was conducted to confirm the usefulness of acid insoluble ash (AIA) as a marker for digestion trials with rabbits. The study compared the fecal excretion of AIA with that of chromic oxide, which has been widely used as an external marker. The diet used was commercial pellets. Water was available
ad libitum. Chemical analysis of AIA was performed by boiling feeds and feces in 4N HCl for 30 min and then ashing the residue at 650°C for 6 hr. The concentrations of AIA in the feeds and feces showed that fecal recovery of AIA was almost complete: 100±3.02 % (mean ± SD,
n=5). This value was approximately equal to that obtained using chromic oxide. Furthermore, there were no differences in apparent digestibility determined by the total collection and AIA ratio methods. In addition, the fecal excretion behavior of AIA was very similar to that of chromic oxide. These results suggest that AIA can be used as an effective marker in digestion studies with rabbits.
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Shigeaki ICHIKAWA, Yoshihiro MURAI, Syuji YAMAMOTO, Yuzo SHIBUYA, Tada ...
1981 Volume 45 Issue 10 Pages
2225-2229
Published: 1981
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Isolation of mutants with an enhanced productivity of 7β-(4-carboxybutanamido)-cephalosporanic acid acylase (penicillin amidohydrolase, EC 3.5.1.11) was attempted. A mutant, Ci-36, isolated by a method using glutarylanilide, produced approximately 5-times more acylase than did the parental strain. However, this acylase formation was still dependent on glutaric acid which was previously found to be essential in the case of the wild strain,
Pseudomonas SY-77-1. The inducible-acylase formation was found to be firmly associated with the process of cell multiplication. Subsequently, a mutant, GK-16 was derived from Ci-36, which was shown to produce the acylase at maximum level without the addition of glutaric acid. The productivity of GK-16 was 2.4-times higher than that of Ci-36.
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Shigeaki ICHIKAWA, Yuzo SHIBUYA, Kunio MATSUMOTO, Tadashiro FUJII, Ken ...
1981 Volume 45 Issue 10 Pages
2231-2236
Published: 1981
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7β-(4-Carboxybutanamido)cephalosporanic acid acylase (penicillin amidohydrolase, EC 3.5.1.11) was crystallized from cell-free extracts of a mutant derived from
Pseudomonas SY-77-1. Purification of the enzyme was performed by a procedure involving ammonium sulfate fractionation and column chromatographies on DEAE-Sephadex, TEAE-cellulose and Sephadex G-200. The crystalline enzyme was homogeneous on polyacrylamide gel disc electrophoresis. The molecular weight of the acylase was estimated to be 1.3×10
5 by gel filtration. The enzyme was fully active at pH above 6.5 and was highly stable at a pH range of 6.0 to 8.0 and below 38°C . The Michaelis-Menten constant (
Km) and
Vmax for 7β-(4-carboxybutanamido)cephalosporanic acid were 0.16 mM and 4.91 μmol/min/mg-protein, respectively. It was also indicated that this enzyme-protein occupied 2.3 % of the dry-cell weight.
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Takashi HAMANO, Yukimasa MITSUHASHI, Yukio MATSUKI
1981 Volume 45 Issue 10 Pages
2237-2243
Published: 1981
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A simple and selective gas chromatographic method was established for determining naturally occurring secondary amines. Secondary amines separated from foods by extraction with dichloromethane and reextraction with hydrochloric acid were readily converted into the corresponding sulfonamides by reaction with benzenesulfonyl chloride under alkaline condition. Gas chromatography was carried out with a capillary coated with OV-101 and a flame photometric detector. Column temperature was programmed from 170 to 230°C at a rate of 5°C/min.
The obtained sulfonamides were separated from one another within 40 min.
Eleven secondary amines examined were added to 5 kinds of foods and recovered from them. The mean recovery rates were in the range 71.3 % (dimethylamine)-99.8 % (piperidine).
The limits of detection varied from 0.002 ppm (dimethylamine) to 0.01 ppm (morpholine).
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Hitoshi AOSHIMA, Tadahiko KAJIWARA, Akikazu HATANAKA
1981 Volume 45 Issue 10 Pages
2245-2251
Published: 1981
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The decomposition of lipid hydroperoxide by soybean lipoxygenase-1 (EC 1.13.11.12) under aerobic conditions was studied by high performance liquid chromatography and the spin trapping method. The reaction followed first order kinetics for lipid hydroperoxide. Its rate was proportional to the enzyme concentration and was independent of pH. A decrease in reactivity due to thermal denaturation and H
2O
2-modification of the enzyme indicated that native lipoxygenase was involved in the decomposition of the lipid hydroperoxide. The free radical, possibly the alkyl radical, was trapped by a radical scavenger, 2-methyl-2-nitrosopropane, in the mixture of soybean lipoxygenase-1 and the lipid hydroperoxide. These results indicated a free-radical chain reaction mechanism for decompositon of the lipid hydroperoxide initiated by soybean lipoxygenase-1.
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Satoshi TAHARA, Zainuddin HAFSAH, Akira ONO, Etsuko ASAISHI, Junya MIZ ...
1981 Volume 45 Issue 10 Pages
2253-2258
Published: 1981
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Metabolism of 2, 4-dichloro-1-nitrobenzene (1) by
Mucor javnicus AHU 6010 was investigated. In addition to the corresponding benzenamine derivative (2), two novel metabolites detected gas-chromatographically were extracted from the culture medium and isolated. The structures were unequivocally elucidated to be 4-chloro-2-methylthio-1-nitrobenzene (3) and 4-chloro-2-methyl-thiobenzenamine (4), respectively, by direct comparisons with authentic compounds. It was suggested that two biological reactions, namely, reduction of the nitro group and/or substitution of the
ortho-chlorine atom by a methylthio group, were responsible for the formation of these metabolites.
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Tsutomu IKEDA, Takashi MATSUMOTO, Yukiteru OBI, Takuro KISAKI, Masao N ...
1981 Volume 45 Issue 10 Pages
2259-2263
Published: 1981
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Characteristic differences were examined between tobacco cell strains producing high levels of ubiquinone (UQ) and the original tobacco cell line (
Nicotiana tabacum L. cv BY-2). The growth rate of strains producing high levels of UQ was about half of that of the original cells. The maximum yield in cell dry weight was about two-thirds of that of original cells. The time-course of UQ formation by selected strains and the respiratory rates were similar to those in the original cells. The UQ contents were much higher than those in original cells, not only per g-dry weight but also per cell. Most UQ in the selected strains were also localized in mitochondria, as well as in the original cells. On protein basis, the yield of purified mitochondria from strains producing high levels of UQ was 4.3 times as much as that from original cells. UQ formation per mg of mitochondrial protein and the molar ratios of UQ to the other electron transport components in selected cells were similar to those in original cells. The ratio of the mitochondrial protein yield in strains producing high levels of UQ to the yield in original cells correlated closely with the ratio of UQ content per g-dry weight in UQ-producing strains to UQ content in original cells.
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Tadashi NOGUCHI, Naoyuki NISHIZAWA, Muneo ITOH, Yukio YANAGI, Shin-ich ...
1981 Volume 45 Issue 10 Pages
2265-2272
Published: 1981
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The acid soluble peptide fraction was prepared from rat skeletal muscle, and the amino acid composition of the fraction was analyzed. The peptide fraction was rich in glutamic acid (or glutamine) and glycine and was poor in branched chain or aromatic amino acids. Since the peptide fraction contained N
τ-methylhistidine, the fraction or at least a part of it was presumed to be composed of intermediate peptides of protein degradation in skeletal muscle. At least 31 spots were detected in the fraction by one dimensional paper electrophoresis.
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Shigeru UTSUMI, Tomohiko MORI
1981 Volume 45 Issue 10 Pages
2273-2276
Published: 1981
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The molecular species of legumin from broad bean seeds exhibit wide heterogeneity [S. Utsumi and T. Mori,
Biochim. Biophys. Acta, 621, 179 (1980)]. The subunit compositions of these molecular species were analyzed according to the following procedure: the molecular species were separated by polyacrylamide gel electrophoresis, and then their subunit compositions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The results indicated that five groups with nine kinds of submolecular species having different molecular weights and subunit compositions were present as legumin in the broad bean. According to these results, we have demonstrated the presence of another group consisting of two kinds of submolecular species, in addition to the four groups and seven kinds of submolecular species reported previously. Various possible molecular species of legumin composed of subunit groups classified according to size were presented.
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Yoshimitsu YAMAZAKI, Hidekatsu MAEDA
1981 Volume 45 Issue 10 Pages
2277-2288
Published: 1981
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Three polymerizable NAD derivatives,
N6-[
N-(6-methacrylamidohexyl)carbamoylmethyl]-,
N6-[
N-[2-[
N-(2-methacrylamidoethyl)carbamoyl]ethyl]carbamoylmethyl]-, and
N6-[
N-[
N-(2-hydroxy-3-methacrylamidopropyl)carbamoylmethyl]carbamoylmethyl] -NAD, were synthesized and radically copolymerized with various comonomers [acrylamide,
N-(2-hydroxyethyl)-,
N-ethyl-,
N,
N-diethyl-, and
N,
N-dimethylacrylamide, acrylic acid, and 6-methacrylamidohexylammonium chloride] to give 21 new polymer derivatives of NAD. The monomeric and polymeric NAD derivatives were all coenzymically active against alcohol, lactate, and malate dehydrogenase. The coenzymic activities were affected most strongly by the chemical property of the spacer, accompanied by a regular decrease in
Km versus increasing spacer hydrophobicity. The chemical property of the polymer body also affected the coenzymic activities; the hydrophobic polymer bodies (copolymers with
N,
N-diethyl- and
N,
N-dimethylacrylamide) were efficient as NAD carriers for lactate and malate dehydrogenase, and the positively charged one (copolymer with acrylamide plus 6-methacrylamidohexylammonium chloride) led to good coenzymic activities of the polymeric NAD derivative against all three dehydrogenases. The effects of the NAD density and average molecular weight of the polymer derivatives were also tested.
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Kiyoshi HAYASHI, Takafumi KASUMI, Naoya KUBO, Nobuzo TSUMURA
1981 Volume 45 Issue 10 Pages
2289-2300
Published: 1981
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Streptomyces rutgersensis H-46 isolated from soil produced a lytic enzyme noninducibly. This enzyme was active against
Streptococcus faecalis, and termed SR-1 enzyme. SR-1 enzyme was purified from the cultivation broth to an electrophoretically homogeneous state as rod-shaped crystals. The molecular weight of SR-1 enzyme was estimated to be 22, 000 by gel filtration in the presence of 6 M guanidine-hydrochloride and SDS-polyacrylamide gel electrophoresis, and the isoelectric point was 9.19 by the isoelectric focusing method. SR-1 enzyme was relatively stable in a pH range of 47 and below 60°C, and showed maximum activity at pH 6.0, 48°C and at ionic strength 0.003 for lyophilized whole cells of
S. faecalis. From analysis of digestion products with SR-1 enzyme, the enzyme was considered to be a kind of
N-acetylmuramidase. The amino acid composition was also analyzed.
The lytic spectra of the enzyme was investigated in 46 strains of species thought to be food putrefying microorganisms.
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Takashi YAMADA, Kenji SAKAGUCHI
1981 Volume 45 Issue 10 Pages
2301-2309
Published: 1981
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Cells of the nitrogen-fixing bacterium
Azotobacter vinelandii and the unicellular cyanobacterium
Anacystis nidulans were introduced into protoplasts of
Saccharomyces cerevisiae by the polyethylene glycol (PEG) method. Factors influencing the uptake frequency were examined, and experimental conditions were established for maximizing the uptake frequency. Under optimal conditions, each protoplast took-up a few bacterial cells. Electron-microscopic studies showed the localization of integrated bacterial cells in membrane-bound vesicles of the cytoplasm or large vacuoles. The protoplasts at the intermediate stages of uptake revealed two major mechanisms of uptake: (a) "endocytosis" by a single protoplast and (b) "cell fusion" between two or more protoplasts. Some bacterial cells disintegrated during the subsequent incubation period through a heterophagy-like process.
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Kazuo AISAKA, Osamu TERADA
1981 Volume 45 Issue 10 Pages
2311-2316
Published: 1981
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The distribution of galactose oxidase was investigated among microorganisms.
Gibberella fujikuroi excreted a large amount of the enzyme into the culture medium. A study of the cultural conditions of this organism for enzyme formation showed that galactose oxidase production required copper. Copper was found to play a role, not only in the conversion of apoenzyme to holoenzyme, but also in regulation of the biosynthesis of galactose oxidase protein.
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Toshiake MATSUZAKI, Akira KOIWAI, Nobumaro KAWASHIMA, Susumu MATSUYAMA
1981 Volume 45 Issue 10 Pages
2317-2321
Published: 1981
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Changes in the lipid components of tobacco leaves during air-curing were investigated. In the air-curing system the contents of total fatty acids and linolenic acid decreased markedly. Digalactosyldiglyceride, monogalactosyldiglyceride, sulfoquinovosyldiglyceride and phosphatidylglycerol, which are components of chloroplast membranes, were degraded almost completely during the process. Phosphatidylethanolamine, phosphatidylserine, phosphatidylcholine (PC) and phosphatidylinositol (PI) were relatively resistant to the degradation process during the yellowing stage, but they also decreased markedly thereafter. PC and PI remained until the final drying stage, although their contents were low. In most polar lipids a considerable decrease was observed in the ratio of linolenic acid. Free fatty acid content increased gradually.
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Hiroshi WATANABE, Hiroshi IIZUKA, Masaaki TAKEHISA
1981 Volume 45 Issue 10 Pages
2323-2327
Published: 1981
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The intact cells of
M. radiodurans were rendered sensitive to the action of lytic enzyme (P2-2 enzyme) by irradiation. The radiation-induced enhancement of cell lysis with P2-2 enzyme was completely prevented by the addition of
t-butanol and irradiation at liquid nitrogen temperature. These results indicate that the enhancement is due to indirect action resulting from OH radicals. Cell lysis by lysozyme was enhanced only when the cells were irradiated under N
2O. The enhancement of cell lysis with lysozyme was also prevented by adding alcohols. On the other hand, when lipid components in cells were removed by extraction with
n-butanol, the radiation-induced enhancement of cell lysis with P2-2 enzyme and lysozyme was not observed. From these results it is concluded that the enhancement of enzymatic cell lysis by irradiation is attributable to alteration in the lipid-rich layer of the cell wall caused by OH radicals.
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Tomoya OGAWA, Satoru NAKABAYASHI
1981 Volume 45 Issue 10 Pages
2329-2335
Published: 1981
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Five model di- and tri-saccharides corresponding to the part structures of the glycan of glycopeptides were synthesized with regio- and stereo-control. They were as follows: methyl 3-
O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-α-D-mannopyranoside, methyl 4-
O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-α-D-mannopyranoside, methyl 6-
O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-α-D-mannopyranoside, methyl 3, 6-di-
O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-α-D-mannopyranoside, and methyl 2, 4-di-
O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-α-D-mannopyranoside. Some aspects of
1H- and
13C-NMR data of these synthetic saccharides were also described.
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Yohei NATORI, Toshimitsu KAMEI, Tomohisa NAGASAKI
1981 Volume 45 Issue 10 Pages
2337-2338
Published: 1981
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ohei ODA, Takao TERASHITA, Matashi KONO, Sawao MURAO
1981 Volume 45 Issue 10 Pages
2339-2340
Published: 1981
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Akira KONNO, Masaru MIYAWAKI, Masaru MISAKI, Katsuharu YASUMATSU
1981 Volume 45 Issue 10 Pages
2341-2342
Published: 1981
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Tae Ho LEE, Motoo ARAI, Sawao MURAO
1981 Volume 45 Issue 10 Pages
2343-2345
Published: 1981
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Atsushi HATTORI, Keijiro ISHIBASHI
1981 Volume 45 Issue 10 Pages
2347-2349
Published: 1981
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Hiroshi DOI, Fumio IBUKI, Masao KANAMORI
1981 Volume 45 Issue 10 Pages
2351-2353
Published: 1981
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Masahiro OHSUGI, Yasuko INOUE
1981 Volume 45 Issue 10 Pages
2355-2356
Published: 1981
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Keishi SHIMOKAWA
1981 Volume 45 Issue 10 Pages
2357-2359
Published: 1981
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Fumiyasu ISHIKAWA, Kunio OISHI, Ko AIDA
1981 Volume 45 Issue 10 Pages
2361-2362
Published: 1981
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Rikisaku SUEMITSU, Akihiko NAKAMURA
1981 Volume 45 Issue 10 Pages
2363-2364
Published: 1981
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Masayoshi IWAHARA, Motoyoshi HONGO
1981 Volume 45 Issue 10 Pages
2365-2367
Published: 1981
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Hitoshi KONDO, Hiroshi NAKATANI, Keitaro HIROMI
1981 Volume 45 Issue 10 Pages
2369-2370
Published: 1981
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Manabu NUKINA, Takeshi SASSA, Michimasa IKEDA, Kazue TAKAHASHI, Shiger ...
1981 Volume 45 Issue 10 Pages
2371-2373
Published: 1981
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Yukio NAKAMURA, Yoshimi MAEKAWA, Satoko KATAYAMA, Yuji OKADA, Fumiaki ...
1981 Volume 45 Issue 10 Pages
2375-2377
Published: 1981
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Toshiake MATSUZAKI, Akira KOIWAI, Nobumaro KAWASHIMA
1981 Volume 45 Issue 10 Pages
2379-2380
Published: 1981
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Naoshi NAKAGAWA, Karl J. KRAMER, Kenji MORI
1981 Volume 45 Issue 10 Pages
2381-2382
Published: 1981
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Sawao MURAO, Noriaki TANAKA
1981 Volume 45 Issue 10 Pages
2383-2384
Published: 1981
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Nobuji NAKATANI, Reiko INATANI
1981 Volume 45 Issue 10 Pages
2385-2386
Published: 1981
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Takashi TANAKA, Eiji ONO, Masaru ISHIHARA, Shigeru YAMANAKA, Koichi TA ...
1981 Volume 45 Issue 10 Pages
2387-2389
Published: 1981
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Eiji ICHISHIMA, Eiji MAJIMA, Makoto EMI, Kazuya HAYASHI, Sawao MURAO
1981 Volume 45 Issue 10 Pages
2391-2393
Published: 1981
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Eiko TSUCHIYA, Akio TSUBOSHITA, Kazuo KAMIMURA, Tokichi MIYAKAWA, Saku ...
1981 Volume 45 Issue 10 Pages
2395-2396
Published: 1981
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Haruyuki OHKISHI, Daikichiro NISHIKAWA, Hidehiko KUMAGAI, Hideaki YAMA ...
1981 Volume 45 Issue 10 Pages
2397-2398
Published: 1981
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Toshiyuki SUZUKI, Shinji IIJIMA, Takashi SAIKI, Teruhiko BEPPU
1981 Volume 45 Issue 10 Pages
2399-2400
Published: 1981
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Yasuhiro KIKUCHI, Koji YODA, Makari YAMASAKI, Gakuzo TAMURA
1981 Volume 45 Issue 10 Pages
2401-2402
Published: 1981
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