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Yoshiki YAMASAKI, Yukio SUZUKI, Junjiro OZAWA
1977 Volume 41 Issue 9 Pages
1553-1558
Published: 1977
Released on J-STAGE: November 27, 2008
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An α-glucosidase has been isolated from the mycelia of
Mucor racemosus, by a procedure including extraction with urea, fractionation with acetone, treatment with MnCl
2, and successive separation on columns of DEAE-cellulose and SP-Sephadex C-50. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis, gel electrofocusing and ultracentrifugation. The sedimentation constant (
So20, W) of the enzyme was 6.2 S, and its molecular weight was between 114, 000 and 97, 000. The pH optimum of the enzyme was in the pH range of 4.0 to 6.0, and the temperature optimum was 50°C. The purified enzyme was stable in the pH range of 4.0 to 7.0, and also stable up to 45°C. The enzyme also catalyzed the transfer of α-glucosyl residue from maltose to riboflavin.
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Yoshiki YAMASAKI, Yukio SUZUKI, Junjiro OZAWA
1977 Volume 41 Issue 9 Pages
1559-1565
Published: 1977
Released on J-STAGE: November 27, 2008
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The substrate and inhibitor specificities, and α-glucosyltransfer products of the purified α-glucosidase from the mycelia of
Mucor racemosus were investigated. The enzyme hydrolyzed maltose, maltotriose, phenyl α-maltoside, isomaltose, soluble starch, and amylose liberating glucose, but did not act on sucrose. The enzyme hydrolyzed phenyl α-maltoside into glucose and phenyl α-glucoside. Maltotriose was the main α-glucosyltransfer product formed from maltose, and isomaltose was that from soluble starch. Tris and turanose inhibited the enzyme activity, but PCMB and EDTA did not. The enzyme hydrolyzed amylose liberating α-glucose. The enzyme was a glycoprotein containing 4.1% of neutral sugar. The neutral sugar was identified as mannose in the acid hydrolyzate of the enzyme.
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Satoshi UEHARA, Kiyozo HASEGAWA, Mikiro TADA, Michiyo MURATA, Tetsuya ...
1977 Volume 41 Issue 9 Pages
1567-1574
Published: 1977
Released on J-STAGE: November 27, 2008
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Lysophospholipase (EC 3. 1. 1. 5) from the culture broth of
Corticium centrifugum was purified 92-fold in specific activity by DEAE-Sephadex and hydroxylapatite column chromatography. The isoelectric point was at about pH 3.9, and the molecular weight was about 130, 000. The optimal pH was about 3.5_??_5.0. The stable pH range was from 7.0 to 8.0. Lysophospholipase activity was inhibited by Fe
3+, Hg
2+ and Al
3+, but stimulated by various organic solvents. Diazobenzene
p-sulfonic acid, N-bromosuccinimide and diisopropyl-fluorophosphate also inhibited the activity. This enzyme did not hydrolyze mono-, di- or tripalmitin or phosphatidylcholine. Apparent Michaelis constants of lysophospholipase activity for 1-acyl-LPC, 1-palmitoyl-LPC and 1-oleoyl-LPC were 0.35, 0.16 and 0.09mM, respectively. The effect of detergents on the enzyme activity was observed to differ with the fatty acid composition of substrate.
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Masaki SAKAKIBARA, Hajime NOGUCHI
1977 Volume 41 Issue 9 Pages
1575-1580
Published: 1977
Released on J-STAGE: November 27, 2008
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In order to clarify the interaction of the 11 S fraction of soybean proteins with calcium ion, the volume change associated with the interaction was measured with a dilatometer. When CaCl
2 was added to 11 S protein solution, there appeared a volume increase to a constant saturated value with increasing CaCl
2 concentration. Then, the volume decreased at the concentration above 0.04M CaCl
2. On the other hand, the binding of calcium ion to 11 S protein was determined by gel filtration at pH 6.0, 7.0 and 8.0. The number of Ca
2+ ion bound to 11 S protein was evaluated to be 4 to 11 depending on CaCl
2 concentration in 0.02M Tris-HCl and 0.18M KCl solution at pH 8.0. However, the binding was not observed at pH 6.0 and 7.0 By CD measurements it was shown that the addition of 0.05M CaCl
2 to the protein solution did not cause any change in the secondary structure of the protein molecules.
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Yoshio FURUTANI, Izumi TSUCHIYA, Hiroshi NAGANAWA, Tomio TAKEUCHI, Ham ...
1977 Volume 41 Issue 9 Pages
1581-1585
Published: 1977
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Biosynthetic pathway of reticulol was studied by
13C-NMR spectroscopy on
13C-labeled compound and degradation experiment of
14C-labeled compound. The results indicated that the carbon skeleton of the reticulol molecule was the polyacetate in origin and the methoxy group of reticulol was derived from the methyl of methionine.
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Yoshio FURUTANI, Tomio TAKEUCHI, Hamao UMEZAWA
1977 Volume 41 Issue 9 Pages
1587-1592
Published: 1977
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Inhibition mechanism of rat cerebral cortex cyclic nucleotide phosphodiesterases (PDE) by reticulol was investigated. The inhibition of PDE by reticulol was not reduced in the presence of excess PDE activating factor (PAF) or/and Ca
2+ ion. Reticulol showed lower
Ki values for Ca
2+-PAF dependent PDE than for Ca
2+ independent PDE.
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Masaru MATSUO, Tsuneo YASUI, Tatsuyoshi KOBAYASHI
1977 Volume 41 Issue 9 Pages
1593-1599
Published: 1977
Released on J-STAGE: November 27, 2008
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A βxylosidase of a thermophilic fungus,
Malbranchea pulchella var.
sulfurea No. 48, was purified 99-fold from the culture filtrate after ammonium sulfate fractionation, DEAE-cellulose column chromatography, column electrophoresis and gel filtration on Sephadex G-200. The purified enzyme was found to be homogeneous upon ultracentrifugal analysis, disc electrophoresis and gel filtration. The molecular weight of the enzyme was estimated to be 26, 000 by gel filtration, and the sedimentation coefficient was calculated to be 2.78 S.
E1%1cm at 280 nm in phosphate buffer (pH 6.7) was 13.2. The optimum pH was found to be in the range of 6.2_??_6.8, and the optimum temperature was 50°C.
View full abstract
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Masaru MATSUO, Tsuneo YASUI, Tatsuyoshi KOBAYASHI
1977 Volume 41 Issue 9 Pages
1601-1606
Published: 1977
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Some enzymatic properties of
Malbranchea β-xylosidase were investigated. The β-xylosidase activity was inhibited by Hg
2+, Zn
2+, Cu
2+, N-bromosuccinimide,
p-chloromercuri-benzoate and sodium laurylsulfate, while this activity was activated by Ca
2+. The enzyme released xylose as the end product even from 10% xylobiose solution without forming any xylooligosaccharides. The enzyme well acted on aryl-β-D-xylosides, but showed no activity on alkyl-β-D-xylosides, and it was practically free from glucosidase activity. The
Km and
Vmax, values of this enzyme for xylobiose were calculated to be 2.86×10
-3M and 34.5 μmoles/mg/min, respectively, and these values determined for phenyl-β-D-xyloside were 3.01×10
-3M and 16.2 μmoles/mg/min, respectively.
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Teisuke FURUYA, Terukazu NAGUMO, Toshihiro ITOH, Hiroshi KANEKO
1977 Volume 41 Issue 9 Pages
1607-1612
Published: 1977
Released on J-STAGE: November 27, 2008
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A thermophilic acidophilic bacterium was isolated from Owaku-dani hot springs of Izu-Hakone National Park in Japan. This bacterium grows optimally at a temperature of 70°C and a pH of 2_??_3. The isolate was generally spherical in shape, with a diameter of about 0.8_??_1.2 μm, being gram-negative and nonmotile. The DNA base composition was 44%. guanine plus cytosine. Chromatographic, chemical and infrared spectroscopic analysis of the total cellular lipid showed that the lipid constituents contained mainly ether linkages; long chain fatty acids and derivatives were absent. The data presented suggests that the thermophilic acidophilic isolate may have some relationship to the
Sulfolobus.
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Yasuo NAKAMURA, Kanji ISHIKAWA, Shozo KUWATSUKA
1977 Volume 41 Issue 9 Pages
1613-1620
Published: 1977
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The metabolic fate of
14C-benthiocarb in rice and barnyard millet at the 4-leaf stage was studied. Benthiocarb was degraded rapidly after absorption through the root. Most of the radioactivity in the plants was extracted with aqueous acetone. The radioactivity in the water-soluble fraction and the aqueous acetone-unextractable residue increased with decreasing benthiocarb. Desethyl benthiocarb,
S-4-chlorobenzyl thiocarbamate, 4-chlorobenzoic acid, 2-hydroxybenthiocarb, desethyl 2-hydroxybenthiocarb, 4-chloro-2-hydroxybenzyl alcohol and 4-chlorosalicylic acid were identified as the metabolic products by thin-layer chromatography. Five of them having hydroxy group and/or carboxyl group, and 4-chlorobenzyl alcohol were also found as conjugation products. The same metabolic products were also found in both the root and foliage of both plants. There was little difference in the metabolic pattern of both plants.
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Shuhei KUBOTA, Eiji TANIGUCHI, Morifusa ETO, Kazuyuki MAEKAWA
1977 Volume 41 Issue 9 Pages
1621-1625
Published: 1977
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A number of new 1, 3-dithiane-2-thione derivatives were synthesized from bismesylates of substituted 1, 3-dihydroxypropanes by the reaction with sodium trithiocarbonate provided from Na
2S and CS
2.
The cyclic structures were elucidated on the basis of the IR, UV, NMR, and mass spectra, together with elemental analyses and chemical reactions.
View full abstract
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Shizuya TANAKA, Toshiro KATO, Shigeo YAMAMOTO, Hirosuke YOSHIOKA
1977 Volume 41 Issue 9 Pages
1627-1633
Published: 1977
Released on J-STAGE: November 27, 2008
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Fungicidal activities of S-alkyl S'-
p-substituted benzyl N-3-pyridyldithiocarbonimidates toward
Coniothyrium diplodiella, Scleotinia sclerotiorum (on agar medium) and
Sphaerotheca fuliginea (on pot test) were shown. The activities varied with the change of the S-alkyl group and were maximized at certain numbers of carbon atoms.
A different pattern was observed in the activity toward
S. fuliginea when the carbon number was 8 or more. Bulkiness of the S-alkyl group also appeared to influence the activities. The steric factor of the
p-alkyl substituents mainly influenced the activity toward
S. fuliginea up to the
tert-butyl analog. The activities toward
C. diplodiella and
S. sclerotiorum increased with the increase in the bulkiness and the hydrophylicity of the
p-substituent.
RM values were determined on reversed phase TLC and the structure-activity correlations were analyzed against hydrophobic (
RM), electronic (σ) and steric (Es) factors on 34 compounds.
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Satoshi TAHARA, Shin KUROGOCHI, Masaki KUDO, Junya MIZUTANI
1977 Volume 41 Issue 9 Pages
1635-1642
Published: 1977
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The metabolism of sorbic acid (SA) by 11 species of
Mucor and 14 other fungi in addition to
Mucor sp. A-73 were studied. All species of
Mucor metabolized SA to
trans-4-hexenol (4-HEL) without exception. The metabolic pathway was investigated precisely by using the resting cells of
Mucor sp. A-73. The reduction of SA to 4-HEL by the fungus demanded glucose. The reduction of SA to sorbic alcohol (SAL) was catalyzed by the inducible enzymic system and that of SAL to 4-HEL by the constitutive enzyme. In the phosphate buffer, a part of 4-HEL produced from SA was further transformed into mono-
trans-4-hexenyl phosphate by
Mucor sp. A-73.
The reductive action of the fungus upon several
trans-2-alkenoic acids was also examined.
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Satoshi TAHARA, Yumiko SUZUKI, Junya MIZUTANI
1977 Volume 41 Issue 9 Pages
1643-1650
Published: 1977
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The metabolisms of
trans-2-octenoic acid (2-OEA) and related compounds were investigated by using one of
Mucor species which could reduce sorbic acid to
trans-4-hexenol. In a phosphate buffer solution, 3-hydroxyoctanoic acid (3-HOA), monooctyl phosphate (OLP), 1-octanol and 1, 3-octanediol were produced as metabolites of 2-OEA. It was elucidated that the conversion of 2-OEA into 3-HOA was reversible and finally most of the substrate was transformed into OLP via the following pathway: 3-HOA_??_2-OEA→
trans-2-octenol→1-octanol→OLP. Similarly,
trans-3-octenol and mono-
trans-3-octenyl phosphate were produced by the fungus as major metabolites of
trans-3-octenoic acid.
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Takashi SAIKI, Ken YAMAZUMI, Kei ARIMA
1977 Volume 41 Issue 9 Pages
1651-1655
Published: 1977
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Aspartokinase (ATP: L-aspartate 4-phosphotransferase) was extracted and partially purified 11-fold from an extreme thermophile,
Thermus flavus AT-62. The enzyme has a temperature optimum near 75°C and a pH optimum of 7 to 8. The enzyme activity was feedback inhibited 80% by L-threonine at the concentration of 0.1mM at 60°C. No concerted effect of L-threonine with any other aspartate family amino acids was observed. The aspartokinase and homoserine dehydrogenase activities were eluted at different concentrations of KCl from DEAE-cellulose column. The aspartokinase was not inactivated after 30min at 70°C, but 30% of the original activity was lost after 30min at 80°C and rapid inactivation occurred above 85°C. The allosteric sensitivity of the enzyme was maintained even at 60_??_80°C but was reduced with the increase of temperature, accompanying desensitization above 80°C. The heat stability of the enzyme activity and of the allosteric sensitivity was discussed in comparison with other allosteric enzymes of thermophiles.
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Tadanobu NAKADAI, Seiichi NASUNO
1977 Volume 41 Issue 9 Pages
1657-1666
Published: 1977
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Leucine aminopeptidase IV in extracts of wheat bran culture of
Aspergillus oryzae 460 was separated from arylamidase by polyacrylamide gel disc electrophoresis at pH 8.0 for 1 hr. The purified enzyme showed neither arylamidase nor amidase activity. The optimum pH was 7.0 on L-leucyl-L-glycyl-L-glycine (Leu-Gly-Gly) as substrate. The enzyme was inhibited by diisopropylphosphorofluoridate (DFP), but not by metal chelating agents. The enzyme molecular weight was estimated to be about 130, 000 by gel filtration method.
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Hiroyuki HORITSU, Toshimi SATAKE, Kiyoshi OGAWA, Mikio TOMOYEDA
1977 Volume 41 Issue 9 Pages
1667-1672
Published: 1977
Released on J-STAGE: November 27, 2008
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5'-Guanosine monophosphate (5'-GMP) was found to leak from
Candida lipolytica (IFO, 0746) and its mutant Y and Sm.
Mutant Sm obtained from the parent strain by treatment with N-methyl-N'-nitro-N-nitrosoguanidine (NTG) and ultraviolet irradiation was found to leak 5'-GMP at 5 times the amount of the parent strain. The properties of mutant Y and Sm were compared with the parent strain, and differences were present in growth, amount of 5'-GMP leakage and ribonuclease activity.
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Shuji ADACHI, Kazuhiro NAKANISHI, Ryuichi MATSUNO, Tadashi KAMIKUBO
1977 Volume 41 Issue 9 Pages
1673-1678
Published: 1977
Released on J-STAGE: November 27, 2008
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The hydrolysis of maltose by glucoamylase (EC 3. 2. 1. 3 from
Rhizopus niveus) was carried out in the presence and absence of dextran and dextran sulfate, which are the components of supports of immobilized enzymes. The interaction between dextran and the enzyme was observed by the fluorescence spectrophotometry. The kinetic and fluorescence experiments indicated that dextran bound to glucoamylase and was apparently a noncompetitive inhibitor of the enzyme. The dissociation constant of the enzyme-dextran complex was estimated to be 34%. The reaction rate was hardly affected at pH 4.0 and 4.5 by addition of dextran sulfate, while the kinetic parameters depended considerably on the concentration of dextran sulfate at pH 3.5. These findings indicated that there might exist some interactions between the enzyme and dextran sulfate.
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Teruhiko YOSHIHARA, Hiroshi YOSHIKAWA, Shigeo KUNIMATSU, Sadao SAKAMUR ...
1977 Volume 41 Issue 9 Pages
1679-1684
Published: 1977
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The polyphenols in red clover were examined from the standpoint of disease resistance to the northern anthracnose. The polyphenols were identified as
trans-clovamide [N-
trans-caffeoyl-3-(3, 4-dihydroxyphenyl)-L-alanine] (VI),
cis-clovamide [N-
cis-caffeoyl-3-(3, 4-dihydroxyphenyl)-L-alanine] (X) and phaselic acid (
trans-caffeoyl-L-malic acid) (II).
trans-Clovamide and
cis-clovamide are new compounds.
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Harukazu FUKAMI, Hideki KOHNO, Katsuhiko KITAHARA, Minoru NAKAJIMA
1977 Volume 41 Issue 9 Pages
1685-1688
Published: 1977
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4-
O-, 5-
O- and 6-
O-β-D-Ribofuranosyl-2-deoxystreptamine derivatives were prepared from 4 (or 6)-
O-acetyl-
N, N'-dicarbobenzyloxy-2-deoxystreptamine and 2, 3, 5-tri-
O-benzoyl-D-ribofuranosyl chloride by a modified Königs-Knorr reaction. Structures were determined by identification with an authentic sample derived from neomycin for the 5-
O-isomer, and by comparison of the
Δ [M]
CuAm values of their
N-acetyl derivatives for the 4-
O- and 6-
O-isomers.
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Harukazu FUKAMI, Shoji IKEDA, Katsuhiko KITAHARA, Minoru NAKAJIMA
1977 Volume 41 Issue 9 Pages
1689-1694
Published: 1977
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Suitably protected 5-
O-β-D-ribofuranosyl-2-deoxystreptamine was condensed with protected 2, 6-diamino-2, 6-dideoxy-α-D-glucopyranosyl bromide by a modified Königs-Knorr reaction to give three condensation products. One of which was confirmed as a ribostamycin derivative. The others were designated as its 6-
O-α- and 6-
O-β-isomers by the PMR spectra of their free bases and
N-acetyl derivatives and by their chemical reactions.
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Kei YAMANAKA, Kiyokazu IZAWA, Kimiko TENMIZU
1977 Volume 41 Issue 9 Pages
1695-1699
Published: 1977
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Molecular properties of crystalline NAD: D-mannitol dehydrogenase of
Leuconostoc mesenteroides were investigated. The extinction coefficient at 280 nm (
E1%1cm) and the sedimentation coefficient (
s020, W) were determined to be 4.14 and 7.37 s, respectively. The isoelectric point was at pH 3.98 by isoelectric focusing. The molecular weight was estimated to be 137, 000±1, 000 dalton by gel filtration on Sephadex G-200 and Ultrogel AcA 34, and sucrose density gradient centrifugation. The enzyme is consisted of four presumably identical subunits having a molecular weight of 38, 000 dalton. The amino acid composition of the enzyme was determined and characterized the absence of tryptophan in the enzyme molecule.
View full abstract
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Kazuo YONAHA, Seizen TOYAMA, Masaaki YASUDA, Kenji SODA
1977 Volume 41 Issue 9 Pages
1701-1706
Published: 1977
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ω-Amino acid: pyruvate aminotransferase, purified to homogeneity and crystallized from a
Pseudomonas sp. F-126, has a molecular weight of 172, 000 or 167, 000±3000 as determined by the gel-filtration or sedimentation equilibrium method, respectively. The enzyme catalyzes the transamination between various ω-amino acids or amines and pyruvate which is the exclusive amino acceptor. α-Amino acids except L-α-alanine are inert as amino donor. The Michaelis constants are 3.3mM for β-alanine, 19mM for 2-aminoethane sulfonate and 3.3mM for pyruvate. The enzyme has a maximum activity in the pH range of 8.5_??_10.5. The enzyme is stable at pH 8.0_??_10.0 and at up to 65°C at pH 8.0. Carbonyl reagents strongly inhibit the enzyme activity. Pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate reactivate the enzyme inactivated by carbonyl reagents. The inhibition constants were determined to be 0.73mM for D-penicillamine and 0.58mM for D-cycloserine. Thiol reagents, chelating agents and L-α-amino acids showed no effect on the enzyme activity.
View full abstract
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Sadahiro OHMOMO, Kenji MIYAZAKI, Tsutomu OHASHI, Matazo ABE
1977 Volume 41 Issue 9 Pages
1707-1710
Published: 1977
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Experiments on the biosynthesis and microbiological conversion of indole alkaloids in
Penicillium concavo-rugulosum were carried out with the growing and resting mycelia, respectively, of a selected strain of the same mold. The former experiments were performed by the use of DL-tryptophan-3-
14C or DL-mevalonic acid-2-
14C-lactone as a precursor, while the latter experiments by the use of rugulovasine A-
3H, dihydrorugulovasine A-
3H, 4-[γ, γ-dimethylallyl]-tryptophan-
3H, chanoclavine-[I]-
3H or the other tritilated ergoline alkaloids. The results of these experiments suggested that in the
Penicillium mold employed there exist the following biosynthetic route: tryptophan+mevalonic acid→4-[γ, γ-dimethylallyl]-tryptophan→rugulovasine A→dihydrorugulovasine A→dihydrorugulovasine A-lactam.
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Masami NANZYO, Takayuki ORITANI, Kyohei YAMASHITA
1977 Volume 41 Issue 9 Pages
1711-1720
Published: 1977
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For the elucidation of the role of methyl substituents on cyclohexene ring of abscisic acid (ABA, I) on the physiological activity, 2'-demethyl-ABA (II), the two stereoisomers (III and IV) of 6'-demethyl-ABA and methyl 5-(1, ' 6'-epoxy-2', 2'-dimethylcyclohexyl)-3-methyl-(2
Z, 4
E)-2, 4-pentadienoate (VI) were synthesized. From the result of rice seedling assay, it was concluded that 2'-methyl group of ABA was indispensable for strong growth inhibitory activities and that at least one of the 6'-
gem-dimethyl groups was unnecessary for growth inhibition.
View full abstract
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Masao FUJIMAKI, Takashi TSUGITA, Tadao KURATA
1977 Volume 41 Issue 9 Pages
1721-1725
Published: 1977
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Fractionation of the volatile concentrate obtained from steam-distillate of rice bran and organoleptic tests of each fraction were carried out. The neutral fraction gave a much higher yield than others and was assumed to be indispensable for the reproduction of rice bran odor. The acidic fraction methylated with diazomethane and the phenolic fraction were analyzed by glass capillary gas chromatography to identify 17 carboxylic acids and 7 phenols. 4-Vinylguaiacol and 4-vinylphenol identified in the steam volatile concentrate were considered to be produced from ferulic and
p-coumaric acids during steam-distillation. 4-Vinylphenol was the main component in the steam volatile concentrate of rice bran, having a characteristic unpleasant odor.
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Teru ISHIBASHI, Masao KAMETAKA
1977 Volume 41 Issue 9 Pages
1727-1732
Published: 1977
Released on J-STAGE: November 27, 2008
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The lysine requirements of rats of various body weights were estimated using the feeding and isotope tests.
The regression equation obtained by the feeding test was
Y=1.03-0.58log
X. Where
Y is lysine percentage of the diet and
X is the mean of initial and final body weights (g) of rats achieving optimal growth gains during the feeding period.
The regression equation obtained by the isotope test was
Y=0.90-0.49log
X, where
Y and
X are lysine percentage in the diet and body weights (g) of rats achieving optimal growth gains at the injection time respectively.
View full abstract
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Makoto KIMURA, Gunki FUNATSU, Masaru FUNATSU
1977 Volume 41 Issue 9 Pages
1733-1736
Published: 1977
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Twelve tryptic peptides as well as free arginine were isolated from the performic acidoxidized Ala chain of ricin D by gel filtration on Sephadex G-25 and Dowex 1×2 column chromatography followed by paper chromatography. Total number of the amino acid residues in these peptides accounted for 90 out of 263 residues in the Ala chain of ricin D.
The amino acid sequences of nine peptides were determined by manual Edman degradation.
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Gunki FUNATSU, Shigetoshi UENO, Masaru FUNATSU
1977 Volume 41 Issue 9 Pages
1737-1743
Published: 1977
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Two constituent polypeptide chains of castor bean hemagglutinin (CBH-A) were isolated from the performic acid-oxidized or reduced-carboxymethylated CBH-A by chromatography on DEAE-cellulose or Sepharose 4 B.
From the analyses of the N-terminal amino acids, the amino acid compositions and the tryptic peptides of each chain, it was found that the larger chain with mol. wt. 34, 000 and the smaller chain with mol. wt. 31, 000 were homologous with the Ala and Ile chains of ricin D, respectively, and the subunit structure of CBH-A is represented as(α'β')
2 in relation to αβ of ricin D.
View full abstract
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Takeshige HAGIHARA, Masayoshi MISHINA, Atsuo TANAKA, Saburo FUKUI
1977 Volume 41 Issue 9 Pages
1745-1748
Published: 1977
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A hydrocarbon-utilizable yeast,
Candida lipolytica NRRL Y-6795, was found to utilize pristane (2, 6, 10, 14-tetramethylpentadecane) as the sole source of carbon and energy. The maximum cell yield (about 4mg dry cell/ml) was obtained in 6 to 7 days' cultivation on 1% (v/v) pristane. Pristanoic acid (2, 6, 10, 14-tetramethylpentadecanoic acid) was identified as an oxidation product of pristane. Analysis of cellular fatty acids of
C. lipolytica grown on pristane showed that pristanoic acid was contained in neutral lipids as major component and in polar lipids as minor one. Accumulation of pristanoic acid in culture filtrate was not appreciable.
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Yoshiki TANI, Hiroshi MORITA, Koichi OGATA
1977 Volume 41 Issue 9 Pages
1749-1754
Published: 1977
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Some enzymatic activities which may be possibly involved in biosynthesis of glycolaldehyde, a precursor of vitamin B
6, were sought in the cell-free extracts of a wild type and a vitamin B
6 auxotroph of
Escherichia coli B. The cell-free extract from the auxotroph had no activity of NADP dependent glycolaldehyde dehydrogenase, while that of wild type strain showed enough of its activity. No significant difference in other possible enzymatic activities were observed between the two strains. Glycolaldehyde stimulates the growth of the auxotroph as pyridoxal does, while glycolate has no effect on it.
From these results, it became apparent that glycolaldehyde is synthesized from glycolate in
E. coli B and that glycolaldehyde dehydrogenase is genetically defective in the vitamin B
6 auxotroph.
View full abstract
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Shigehiro HIRANO, Osamu MIURA, Ryuji YAMAGUCHI
1977 Volume 41 Issue 9 Pages
1755-1759
Published: 1977
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A series of partially and heterogeneously
N-acylated chitosans was prepared and isolated in 50_??_100% yields. The structure of
N-acyl groups influenced the gelation. The minimum requirement for the gelation was defined as
ca. 0.4
N-lauroyl (C
12),
ca. 0.6
N-fatty acyl (C
3-C
10) or
ca. 0.7
N-benzoyl groups per hexosaminide residue. However, the gelation did not occur with
N-high fatty acyl (C
14-C
18) groups.
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Hitomi NAKADA, Akio KOBAYASHI, Kyohei YAMASHITA
1977 Volume 41 Issue 9 Pages
1761-1765
Published: 1977
Released on J-STAGE: November 27, 2008
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The absolute configuration of a phytoalexin “Safynol” (3
E, 11
E)-3, 11-tridecadiene-5, 7, 9-triyne-1, 2-diol (I), separated from
Phytophthora drechsleri-infected safflower (
Carthamus tinctorius L.) was confirmed. (
R) and (
S)-safynol were synthesized from 2, 3-O-isopropyli-dene-(
S)- and (
R)-glyceraldehyde respectively, and the (
R) configuration was assigned to the natural product. The inhibitory effects of (
R)- and (
S)-safynol on mycelial growth of five fungi were almost the same and their ED
50 values ranged from 6 to 70 ppm.
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Motoo SHIBATA, Masaru UYEDA, Yutaka KIDO, Keiko SHIGEMORI, Yoko AZIKI, ...
1977 Volume 41 Issue 9 Pages
1767-1771
Published: 1977
Released on J-STAGE: November 27, 2008
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From the results of taxonomic studies,
Streptomyces sp. strain No. KT-151 isolated from a soil sample collected in Kumamoto City, was identified as a strain belonging to
Streptomyces luteogriseus Schmitz, Deak, Crook and Hooper 1964.
A new antibiotic, produced by this strain, was isolated as a leaflet crystal by ion-exchange chromatography and found to be an amino acid with the molecular formula, C
5H
12N
2O
2, and named antibiotic KT-151 (refered to as KT-151 hereinafter). The antibiotic showed antimicrobial activity against various Gram-positive and Gram-negative bacteria in a chemically defined medium but it was antagonized by several amino acids such as valine, leucine, isoleucine and threonine.
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Hiroshi OHRUI, Sakae EMOTO
1977 Volume 41 Issue 9 Pages
1773-1778
Published: 1977
Released on J-STAGE: November 27, 2008
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An optically active key intermediate, methyl 2, 4-dideoxy-4-
C-carboxymethylene-α-D-
ribo-hexopyranoside 2'→3 lactone (XII), for the syntheses of optically active Thromboxanes was prepared from D-glucose.
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Akira ISOGAI, Shigeo MURAKOSHI, Akinori SUZUKI, Saburo TAMURA
1977 Volume 41 Issue 9 Pages
1779-1784
Published: 1977
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Cinnzeylanine (
1) and cinnzeylanol (
2) were isolated from barks of
Cinnamonum zeylanicum Nees (ceylon cinnamon). Chemical properties and NMR spectra of the both compounds are disccused in terms of their structures which were determined by the X-ray analysis and chemical reactions. When administered orally with artificial diet, both
1 and
2 killed larvae of silkworm,
Bombyx mori L. at a dose of 16 ppm and inhibited larval ecdysis at 2_??_4 ppm.
View full abstract
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Hiromu KAMEOKA, Chi-Pao WANG, Kenji TOKIMITSU
1977 Volume 41 Issue 9 Pages
1785-1786
Published: 1977
Released on J-STAGE: November 27, 2008
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Hitoshi AOSHIMA, Jiro SEKIYA, Tadahiko KAJIWARA, Akikazu HATANAKA
1977 Volume 41 Issue 9 Pages
1787-1788
Published: 1977
Released on J-STAGE: November 27, 2008
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Takashi KOMIYA, Tetsuya YAMADA, Shozo NARA, Mitsuo NAMIKI
1977 Volume 41 Issue 9 Pages
1789-1790
Published: 1977
Released on J-STAGE: November 27, 2008
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Sachiko ESAKI, Shintaro KAMIYA, Fukuko KONISHI
1977 Volume 41 Issue 9 Pages
1791-1792
Published: 1977
Released on J-STAGE: November 27, 2008
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Tadahiko KAJIWARA, Jiro SEKIYA, Yasuji KIDO, Akikazu HATANAKA
1977 Volume 41 Issue 9 Pages
1793-1794
Published: 1977
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Teru ISHIBASHI, Masao KAMETAKA
1977 Volume 41 Issue 9 Pages
1795-1796
Published: 1977
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Gunki FUNATSU, Shigetoshi UENO, Masaru FUNATSU
1977 Volume 41 Issue 9 Pages
1797-1798
Published: 1977
Released on J-STAGE: November 27, 2008
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Shigeo MURAKAWA, Susumu SANO, Haruo YAMASHITA, Takeshi TAKAHASHI
1977 Volume 41 Issue 9 Pages
1799-1800
Published: 1977
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Shuhei NAKAJIMA, Kazuyoshi KAWAZU
1977 Volume 41 Issue 9 Pages
1801-1802
Published: 1977
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Michimasa IKEDA, Gen-ichi NIWA, Katsumi TOHYAMA, Takeshi SASSA, Yukich ...
1977 Volume 41 Issue 9 Pages
1803-1805
Published: 1977
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Shoji SHIMA, Heiichi SAKAI
1977 Volume 41 Issue 9 Pages
1807-1809
Published: 1977
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Tadashi OGAWA, Masumi KIMOTO, Kei SASAOKA
1977 Volume 41 Issue 9 Pages
1811-1812
Published: 1977
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Akitami ICHIHARA, Yoshiaki NUMATA, Seiji KANAI, Sadao SAKAMURA
1977 Volume 41 Issue 9 Pages
1813-1814
Published: 1977
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Hirozi SUZUKI, Tsutomu IKEDA, Takashi MATSUMOTO, Masao NOGUCHI
1977 Volume 41 Issue 9 Pages
1815-1817
Published: 1977
Released on J-STAGE: November 27, 2008
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