The Experts below are selected from a list of 294 Experts worldwide ranked by ideXlab platform
Fumio Yagi - One of the best experts on this subject based on the ideXlab platform.
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Two carbohydrate recognizing domains from Cycas revoluta leaf lectin show the distinct sugar-binding specificity—A unique mannooligosaccharide recognition by N-terminal domain
Journal of biochemistry, 2016Co-Authors: Michiko Shimokawa, Fumio Yagi, Tomokazu Haraguchi, Yuji Minami, Keiko Hiemori, Hiroaki Tateno, Jun HirabayashiAbstract:Cycas revoluta leaf lectin (CRLL) of mannose-recognizing jacalin-related lectin (mJRL) has two tandem repeated carbohydrate recognition domains, and shows the characteristic sugar-binding specificity toward high mannose-glycans, compared with other mJRLs. We expressed the N-terminal domain and C-terminal domain (CRLL-N and CRLL-C) separately, to determine the fine sugar-binding specificity of each domain, using frontal affinity chromatography, glycan array and equilibrium dialysis. The specificity of CRLL toward high mannose was basically derived from CRLL-N, whereas CRLL-C had affinity for α1-6 extended mono-antennary complex-type glycans. Notably, the affinity of CRLL-N was most potent to one of three Man 8 glycans and Man 9 glycan, whereas the affinity of CRLL-C decreased with the increase in the number of extended α1-2 linked mannose residue. The recognition of the Man 8 glycans by CRLL-N has not been found for other mannose recognizing lectins. Glycan array reflected these specificities of the two domains. Furthermore, it was revealed by equilibrium dialysis method that the each domain had two sugar-binding sites, similar with Banlec, banana mannose-binding Jacalin-related lectin.
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Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds
Peptides, 2008Co-Authors: Seiya Yokoyama, Kouji Kato, Atsuko Koba, Yuji Minami, Keiichi Watanabe, Fumio YagiAbstract:Novel antimicrobial peptides (AMP), designated Cy-AMP1, Cy-AMP2, and Cy-AMP3, were purified from seeds of the cycad (Cycas revoluta) by a CM cellulofine column, ion-exchange HPLC on SP COSMOGEL, and reverse-phase HPLC. They had molecular masses of 4583.2 Da, 4568.9 Da and 9275.8 Da, respectively, by MALDI-TOF MS analysis. Half of the amino acid residues of Cy-AMP1 and Cy-AMP2 were cysteine, glycine and proline, and their sequences were similar. The sequence of Cy-AMP3 showed high homology to various lipid transfer proteins. For Cy-AMP1 and Cy-AMP2, the concentrations of peptides required for 50% inhibition (IC(50)) of the growth of plant pathogenic fungi, Gram-positive and Gram-negative bacteria were 7.0-8.9 microg/ml. The Cy-AMP3 had weak antimicrobial activity. The structural and antimicrobial characteristics of Cy-AMP1 and Cy-AMP2 indicated that they are a novel type of antimicrobial peptide belonging to a plant defensin family.
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comparative analysis of carbohydrate binding properties of two tandem repeat type jacalin related lectins castanea crenata agglutinin and Cycas revoluta leaf lectin
FEBS Journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
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Comparative analysis of carbohydrate‐binding properties of two tandem repeat‐type Jacalin‐related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin
The FEBS journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
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The lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related family.
European journal of biochemistry, 2002Co-Authors: Fumio Yagi, Toshinobu Iwaya, Tomokazu Haraguchi, Irwin J. GoldsteinAbstract:A novel lectin was isolated from leaves of the Japanese cycad, Cycas revoluta Thunb. (gymnosperm), and its characteristics including amino acid composition, molecular mass, carbohydrate binding specificity and partial amino acid sequences were examined. The inhibition analysis of hemagglutinating activity with various sugars showed that the lectin has a carbohydrate-binding specificity similar to those of mannose recognizing, jacalin-related lectins. Partial amino acid sequences of the lysylendopeptic peptides shows that the lectin might have a repeating structure and belong to the jacalin-related lectin family.
Jun Hirabayashi - One of the best experts on this subject based on the ideXlab platform.
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Two carbohydrate recognizing domains from Cycas revoluta leaf lectin show the distinct sugar-binding specificity—A unique mannooligosaccharide recognition by N-terminal domain
Journal of biochemistry, 2016Co-Authors: Michiko Shimokawa, Fumio Yagi, Tomokazu Haraguchi, Yuji Minami, Keiko Hiemori, Hiroaki Tateno, Jun HirabayashiAbstract:Cycas revoluta leaf lectin (CRLL) of mannose-recognizing jacalin-related lectin (mJRL) has two tandem repeated carbohydrate recognition domains, and shows the characteristic sugar-binding specificity toward high mannose-glycans, compared with other mJRLs. We expressed the N-terminal domain and C-terminal domain (CRLL-N and CRLL-C) separately, to determine the fine sugar-binding specificity of each domain, using frontal affinity chromatography, glycan array and equilibrium dialysis. The specificity of CRLL toward high mannose was basically derived from CRLL-N, whereas CRLL-C had affinity for α1-6 extended mono-antennary complex-type glycans. Notably, the affinity of CRLL-N was most potent to one of three Man 8 glycans and Man 9 glycan, whereas the affinity of CRLL-C decreased with the increase in the number of extended α1-2 linked mannose residue. The recognition of the Man 8 glycans by CRLL-N has not been found for other mannose recognizing lectins. Glycan array reflected these specificities of the two domains. Furthermore, it was revealed by equilibrium dialysis method that the each domain had two sugar-binding sites, similar with Banlec, banana mannose-binding Jacalin-related lectin.
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comparative analysis of carbohydrate binding properties of two tandem repeat type jacalin related lectins castanea crenata agglutinin and Cycas revoluta leaf lectin
FEBS Journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
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Comparative analysis of carbohydrate‐binding properties of two tandem repeat‐type Jacalin‐related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin
The FEBS journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
Katsuhiko Kondo - One of the best experts on this subject based on the ideXlab platform.
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adventitious embryo formation derived from zygotic embryos in Cycas revoluta
Plant Biotechnology, 2008Co-Authors: Tsuyoshi Motohashi, Katsuhiko Kondo, Miyoko I TodaAbstract:Numerous adventitious embryos of Cycas revoluta were successfully induced and grown on the mature zygotic embryos in the well-ripe, naked seeds used on Schenk and Hildebrandt (SH) medium supplemented with 3.0% sucrose, 20% coconut milk, 0.6% agar and the growth regulators of 0.20 to 2.00 mg l−1 BAP and 0.00 to 0.20 mg l−1 2,4-D in combination at pH 5.9 42 to 84 days after the beginning of the culture. Maximum proliferation of 88.7±40.5 adventitious embryos per zygotic embryo was obtained on SH basal medium supplemented with 0.20 mg l−1 BAP and 0.02 mg l−1 2,4-D. Root formation was seen on all of the adventitious embryos by continuous culture on the same medium. Each rooted plantlet was isolated individually and then, grew big enough to juvenile stage that had one to three leaves with pinnate leaflets, thick trunk and primary tap root on SH basal medium without any growth regulator 196 days after the beginning of the culture and was ready for acclimatization.
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Structural Differences of Chromosomes in Plants Detected by Fluorescence in situ Hybridization Using Probes of rDNA, Arabidopsis-type Telomere Sequence Repeats and pCrT7-4
Some Aspects of Chromosome Structure and Functions, 2002Co-Authors: Katsuhiko Kondo, Norikazu Tagashira, Magdy Hussein Abd El-twab, Yoshikazu Hoshi, Goro Kokubugata, Yoshito Honda, Kyaw Kyaw KhaungAbstract:The chromosomal sites of 5S rDNA, 45S rDNA and Arabidopsis-iypt telomere sequence repeats characterize individual species and population constitutions in chrysanthemums and cycads and those of Sau3A in spruces. The sites of the telomere sequence repeats in the cycad chromosomes occur not only in the usual terminal regions of chromosome-arms as small dots, but also in several centromeric to proximal regions as relatively large signals. Large signals of the 278 bp DNA segment with respect to Cycas revoluta involved with pCrT7-4. The Y-chromosome of Cycas revoluta was distinct by lack of the large signal of pCrT7-4 and the Arabidopsis-type telomere sequence repeats. A highly conserved chromosomal location of these genes lead to speculation on the karyotype evolution and species property of the chrysanthemum and cycad groups.
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Differential staining and in situ hybridization of nucleolar organizers and centromeres in Cycas revoluta chromosomes
The Japanese Journal of Genetics, 1992Co-Authors: Masahiro Hizume, Fumio Ishida, Katsuhiko KondoAbstract:Nucleolar organizers (NORs) and centromeres in the somatic metaphase chromosomes (2n = 22) of Cycas revoluta Thunb. were differentially stained by silver staining and Cd-staining. Silver deposits (Ag-NORs) were located at the terminal end of the long arm of four submetacentric chromosomes and nine telocentric chromosomes. The maximum number of nucleoli per nucleus was 13. In situ hybridization with biotin-labeled rDNA revealed that rRNA genes were located at the terminal ends of four submetacentric chromosomes and all 12 telocentric chromosomes. Most of the signals of rDNA coincided to Ag-NORs. Differential staining with the DNA base specific fluorochromes indicated that the NORs were GC-rich and the centromeres were AT-rich. The proximal and terminal regions of the telocentric chromosomes were GC-rich. A few interstitial GC- and AT-rich bands were observed in some chromosomes.
Sachiko Nakamura - One of the best experts on this subject based on the ideXlab platform.
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comparative analysis of carbohydrate binding properties of two tandem repeat type jacalin related lectins castanea crenata agglutinin and Cycas revoluta leaf lectin
FEBS Journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
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Comparative analysis of carbohydrate‐binding properties of two tandem repeat‐type Jacalin‐related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin
The FEBS journal, 2005Co-Authors: Sachiko Nakamura, Fumio Yagi, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:Lectins belonging to the jacalin-related lectin family are distributed widely in the plant kingdom. Recently, two mannose-specific lectins having tandem repeat-type structures were discovered in Castanea crenata (angiosperm) and Cycas revoluta (gymnosperm). The occurrence of such similar molecules in taxonomically less related plants suggests their importance in the plant body. To obtain clues to understand their physiological roles, we performed detailed analysis of their sugar-binding specificity. For this purpose, we compared the dissociation constants (K(d)) of Castanea crenata agglutinin (CCA) and Cycas revoluta leaf lectin (CRLL) by using 102 pyridylaminated and 13 p-nitrophenyl oligosaccharides with a recently developed automated system for frontal affinity chromatography. As a result, we found that the basic carbohydrate-binding properties of CCA and CRLL were similar, but differed in their preference for larger N-linked glycans (e.g. Man7-9 glycans). While the affinity of CCA decreased with an increase in the number of extended alpha1-2 mannose residues, CRLL could recognize these Man7-9 glycans with much enhanced affinity. Notably, both lectins also preserved considerable affinity for mono-antennary, complex type N-linked glycans, though the specificity was much broader for CCA. The information obtained here should be helpful for understanding their functions in vivo as well as for development of useful probes for animal cells. This is the first systematic approach to elucidate the fine specificities of plant lectins by means of high-throughput, automated frontal affinity chromatography.
Irwin J. Goldstein - One of the best experts on this subject based on the ideXlab platform.
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The lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related family.
European journal of biochemistry, 2002Co-Authors: Fumio Yagi, Toshinobu Iwaya, Tomokazu Haraguchi, Irwin J. GoldsteinAbstract:A novel lectin was isolated from leaves of the Japanese cycad, Cycas revoluta Thunb. (gymnosperm), and its characteristics including amino acid composition, molecular mass, carbohydrate binding specificity and partial amino acid sequences were examined. The inhibition analysis of hemagglutinating activity with various sugars showed that the lectin has a carbohydrate-binding specificity similar to those of mannose recognizing, jacalin-related lectins. Partial amino acid sequences of the lysylendopeptic peptides shows that the lectin might have a repeating structure and belong to the jacalin-related lectin family.
