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Volume 58, Issue 3
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Yasushi MATSUURA1984 Volume 58 Issue 3 Pages 253-259
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe pectic polysaccharide of kidney bean cotyledons was hydrolyzed by boiling under refluxing with 0.1 M oxalic acid. The product of hydrolysis, a xylogalacturonan, consisted of xylose, galacturonic acid and minor neutral sugars. The molar ratio of xylose-to-galacturonic acid was 48.8:100.
Xylogalacturonan was converted into its reduced and methylated derivative. Hydrolysis of the methylated xylogalacturonan yielded 2, 3, 4-tri-O-methyl-D-xylose, 2, 3, 6-tri-O-methyl-D-galactose and 2, 6-di-O-methyl-D-galactose. Therefore, all xylose residues of the xylogalacturonan were present at non-reducing terminal and attached to the galacturonan chain as ‘stubs’ in one residue. As the xylo-galacturonan was hardly hydrolyzed with polygalacturonases, the side chains were probably equally distributed along the galacturonan chain.
Methylation analysis of the pectic polysaccharide was also performed in the same manner as xylo-galacturonan, and the following compounds were identified: 2, 3, 5-tri-O-methyl-D-fucose, 2, 3, 4-tri-O-methyl-D-xylose, 2, 3-di-O-methyl-D-xylose, 2, 3, 6-tri-O-methyl-D-galactose, 2, 6-di-O-methyl-D-galactose and methylated arabinose. In the pectic polysaccharide of kidney bean cotyledons, xylose residues were present at not only the terminal but also internal positions. In the latter case, fucose may be linked with xylose to form fucosyl-xylose stubs in the galacturonan chain. The distribution of the side chains having the xylose residue on the galacturonan chain was probably the same as that of xylogalacturonan.
Xylogalacturonan was subjected to acetolysis, and a polygalacturonide which was free of xylose and other neutral sugars was obtained. Hydrolysis of the uronide with polygalacturonases indicates that the pectic polysaccharide of kidney bean cotyledons consisted of α-1, 4-linked D-galacturonic acid.View full abstractDownload PDF (529K) -
Satoshi SHIINOKI, Junji TSUTIHASHI, Toyoaki SHIMADA, Yataro NUNOKAWA1984 Volume 58 Issue 3 Pages 261-266
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSα-Amylase (Taka-amylase A: TAA) was adsorbed by proteins abundant in basic amino acids, such as oryzenin, protamin and histone. However, the enzyme was not adsorbed by fibroin, which has few basic amino acids.
The adsorption of various α-amylase onto oryzenin immobilized with Sepharose 6 B was examined. α-Amylase (TAA or Koji α-amylase: KAA) from Aspergillus oryzae was adsorbed onto immobilized oryzenin, but α-amylase from Bacillus subtilis (BSA) was not. α-Amylase (TAA) was adsorbed well onto polylisine, polyhistidine and polyarginine but not onto polyaspartic acid. Anion-exchange resin adsorbed α-amylase (TAA or KAA), but cation-exchange resin did not adsorb it. These results suggest that the reason for α-amylase (TAA or KAA) being adsorbed onto the basic amino acid groups of proteins might be the intermolecular ionic bond.View full abstractDownload PDF (408K) -
Nobuhiro FUKUDA, Yasuhiro HIGA, Yasumasa MAKISHI, Isao CHINEN, Harugor ...1984 Volume 58 Issue 3 Pages 267-272
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThis is the first report that describes the purification and characterization of the lectin from Crotalaria zanzibarica seed. The purification of C. zanzibarica seed lactin was carried out first by fractional precipitation with ammonium sulfate, then by DEAE-cellulose and hydroxyapatite column and finally by affinity column chromatography on acid-treated Sepharose 6 B. The lectin obtained was homogenous on polyacrylamide electrophoresis. It was a glycoprotein in reaction with phenol-H2SO4 assay, and its PI was 5.3 by isoelectricfocusing.
The C. zanzibarica lectin had an equal hemagglutinating activity against rabbit, rat and pig erythrocytes, but did not agglutinate human ABO type erythrocytes. When human erythrocytes were treated with trypsin, the lectin agglutinated O>A=B blood type, but did not agglutinate AB type erythrocytes.
The hemagglutinating activity with rabbit erythrocytes was inhibited by sugars containing a galactose residue, indicating that the lectin belonged to the so-called galactose-specific lectin. Among mono-, di- and oligosaccharides tested, the α-anomer was a better inhibitor than β-anomer, and the hydroxyl group at C-6 of pyranose ring may be essential for inhibition of hemagglutination.View full abstractDownload PDF (976K) -
Eiki DEYA, Kaoru NOJIRI, Seiichirou IGARASHI1984 Volume 58 Issue 3 Pages 273-275
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe transglycosylation of lysozyme on chitin oligosaccharides and lactose was examined. A reaction mixture consisting 2% chitin oligosaccharides, 10% lactose, 1% lysozyme and 0.1M acetate buffer (pH 5.0) was incubated at 37°C for 5 hr. Four oligosaccharides composed of N-acetylglucosamines (NAG) and lactose were synthesized by transglycosylation of lysozyme. These oligosaccharides were isolated by charcoal-Celite column chromatography. Their hydrolysates of permethylated oligosaccharides were ana-lyzed as derivatives of acetylated sugar alcohol by gas chromatography. The oligosaccharides were new compounds which were abbreviated as NAG-lactose, (NAG)2-lactose, (NAG)3-lactose and (NAG)4-lactose. These compounds had the following general structure: β-D-galactopyranosyl-(1→4)-[{β-D-N-acetylglu-cosaminyl-(1→4)}n-β-D-N-acetylglucosaminyl-(1→2)]-D-glucose, where n is 0, 1, 2 or 3.View full abstractDownload PDF (220K) -
Tojiro TSUSHIDA, Tadakazu TAKEO1984 Volume 58 Issue 3 Pages 277-279
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe caffeine content of plucked tea shoots increased 20-50% after 48 hr incubation at 25°C. Theobromine, thought the precursor of caffeine, increased in the initial stage of incubation, then decreased rapidly. The maximum increase in caffeine resulted when the plucked shoots were incubated at 25°C. In shoots thawed after freezing at -25°C for 2 hr, the caffeine content did not increase during incubation at 25°C. RNA, 2', 3'-AMP, 2', 3'-GMP, theobromine and theophylline did not enhance the biosynthesis of caffeine in plucked tea shoots.View full abstractDownload PDF (184K) -
Hiuga SAITO1984 Volume 58 Issue 3 Pages 281-287
Published: 1984
Released on J-STAGE: November 21, 2008
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Shigeo TAMAKI1984 Volume 58 Issue 3 Pages 289-294
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (539K) -
[in Japanese]1984 Volume 58 Issue 3 Pages 325-326
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (209K) -
[in Japanese]1984 Volume 58 Issue 3 Pages 327-328
Published: 1984
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (167K)
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