Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen
The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide de...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 1995-02, Vol.117 (2), p.289-295 |
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container_title | Journal of biochemistry (Tokyo) |
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creator | Hino, K Yamamoto, S Sano, O Taniguchi, Y Kohno, K Usui, M Fukuda, S Hanzawa, H Haruyama, H Kurimoto, M |
description | The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides. |
doi_str_mv | 10.1093/jb/117.2.289 |
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The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/117.2.289</identifier><identifier>PMID: 7608114</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>allergen ; allergens ; Allergens - chemistry ; Amino Acid Sequence ; amino acid sequences ; Antigens, Plant ; Asparagine ; Carbohydrate Conformation ; Carbohydrate Sequence ; carbohydrate structure ; chemical structure ; Chromatography, High Pressure Liquid ; composition ; Cry j I ; Cryptomeria japonica ; glycoprotein ; glycoproteins ; H-NMR ; high performance liquid chromatography ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; nuclear magnetic resonance spectroscopy ; oligosaccharides ; Oligosaccharides - chemistry ; Oligosaccharides - isolation & purification ; Peptide Fragments - chemistry ; Peptide Fragments - isolation & purification ; Plant Proteins - chemistry ; pollen ; Pollen - chemistry ; separation ; spectral analysis ; sugars ; Trees ; Trypsin ; Xylose - analysis</subject><ispartof>Journal of biochemistry (Tokyo), 1995-02, Vol.117 (2), p.289-295</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-a7d7b65b9c338935d45c55c9d18ae42769832cef8faa6d7f4c216c281f4829763</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7608114$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hino, K</creatorcontrib><creatorcontrib>Yamamoto, S</creatorcontrib><creatorcontrib>Sano, O</creatorcontrib><creatorcontrib>Taniguchi, Y</creatorcontrib><creatorcontrib>Kohno, K</creatorcontrib><creatorcontrib>Usui, M</creatorcontrib><creatorcontrib>Fukuda, S</creatorcontrib><creatorcontrib>Hanzawa, H</creatorcontrib><creatorcontrib>Haruyama, H</creatorcontrib><creatorcontrib>Kurimoto, M</creatorcontrib><title>Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides.</description><subject>allergen</subject><subject>allergens</subject><subject>Allergens - chemistry</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Antigens, Plant</subject><subject>Asparagine</subject><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>carbohydrate structure</subject><subject>chemical structure</subject><subject>Chromatography, High Pressure Liquid</subject><subject>composition</subject><subject>Cry j I</subject><subject>Cryptomeria japonica</subject><subject>glycoprotein</subject><subject>glycoproteins</subject><subject>H-NMR</subject><subject>high performance liquid chromatography</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>oligosaccharides</subject><subject>Oligosaccharides - chemistry</subject><subject>Oligosaccharides - isolation & purification</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Plant Proteins - chemistry</subject><subject>pollen</subject><subject>Pollen - chemistry</subject><subject>separation</subject><subject>spectral analysis</subject><subject>sugars</subject><subject>Trees</subject><subject>Trypsin</subject><subject>Xylose - analysis</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1v1DAQhi1EVZbCjSvCp6pIzdbjjzg-oi20RUUcaKWKi-U49jYhiYPtSOy_J6td9TQavc-8Gj0IfQCyBqLYVVdfAcg1XdNKvUIrkKIsaCngNVoRQqFQlD-9QW9T6vYrZewUncqSVAB8hcaNiXV43jXRZIdTjrPNc3QJB4_zs8PbfmfDFEN27YhN37u4dSPexB3u8B32MQz4u5nM6JLD1jUm4oslnHIYXGwN7swUxtaaz3gKy_H4Dp140yf3_jjP0OO3rw-b2-L-583d5st9YQXnuTCykXUpamUZqxQTDRdWCKsaqIzjVJaqYtQ6X3ljykZ6bimUllbgeUWVLNkZOj_0Lq__nV3KemiTdX2_fBrmpKVkCgjwBbw8gDaGlKLzeortYOJOA9F7vbqr9aJXU73oXfCPx965HlzzAh99LnlxyNuU3b-X2MQ_upRMCn379FtfVw8_5DW90Xv-04H3JmizjW3Sj78oAUZAUAoC2H_nXY6I</recordid><startdate>19950201</startdate><enddate>19950201</enddate><creator>Hino, K</creator><creator>Yamamoto, S</creator><creator>Sano, O</creator><creator>Taniguchi, Y</creator><creator>Kohno, K</creator><creator>Usui, M</creator><creator>Fukuda, S</creator><creator>Hanzawa, H</creator><creator>Haruyama, H</creator><creator>Kurimoto, M</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19950201</creationdate><title>Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen</title><author>Hino, K ; Yamamoto, S ; Sano, O ; Taniguchi, Y ; Kohno, K ; Usui, M ; Fukuda, S ; Hanzawa, H ; Haruyama, H ; Kurimoto, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-a7d7b65b9c338935d45c55c9d18ae42769832cef8faa6d7f4c216c281f4829763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>allergen</topic><topic>allergens</topic><topic>Allergens - chemistry</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Antigens, Plant</topic><topic>Asparagine</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>carbohydrate structure</topic><topic>chemical structure</topic><topic>Chromatography, High Pressure Liquid</topic><topic>composition</topic><topic>Cry j I</topic><topic>Cryptomeria japonica</topic><topic>glycoprotein</topic><topic>glycoproteins</topic><topic>H-NMR</topic><topic>high performance liquid chromatography</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Sequence Data</topic><topic>nuclear magnetic resonance spectroscopy</topic><topic>oligosaccharides</topic><topic>Oligosaccharides - chemistry</topic><topic>Oligosaccharides - isolation & purification</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Plant Proteins - chemistry</topic><topic>pollen</topic><topic>Pollen - chemistry</topic><topic>separation</topic><topic>spectral analysis</topic><topic>sugars</topic><topic>Trees</topic><topic>Trypsin</topic><topic>Xylose - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hino, K</creatorcontrib><creatorcontrib>Yamamoto, S</creatorcontrib><creatorcontrib>Sano, O</creatorcontrib><creatorcontrib>Taniguchi, Y</creatorcontrib><creatorcontrib>Kohno, K</creatorcontrib><creatorcontrib>Usui, M</creatorcontrib><creatorcontrib>Fukuda, S</creatorcontrib><creatorcontrib>Hanzawa, H</creatorcontrib><creatorcontrib>Haruyama, H</creatorcontrib><creatorcontrib>Kurimoto, M</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hino, K</au><au>Yamamoto, S</au><au>Sano, O</au><au>Taniguchi, Y</au><au>Kohno, K</au><au>Usui, M</au><au>Fukuda, S</au><au>Hanzawa, H</au><au>Haruyama, H</au><au>Kurimoto, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1995-02-01</date><risdate>1995</risdate><volume>117</volume><issue>2</issue><spage>289</spage><epage>295</epage><pages>289-295</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>7608114</pmid><doi>10.1093/jb/117.2.289</doi><tpages>7</tpages></addata></record> |
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subjects | allergen allergens Allergens - chemistry Amino Acid Sequence amino acid sequences Antigens, Plant Asparagine Carbohydrate Conformation Carbohydrate Sequence carbohydrate structure chemical structure Chromatography, High Pressure Liquid composition Cry j I Cryptomeria japonica glycoprotein glycoproteins H-NMR high performance liquid chromatography Magnetic Resonance Spectroscopy Molecular Sequence Data nuclear magnetic resonance spectroscopy oligosaccharides Oligosaccharides - chemistry Oligosaccharides - isolation & purification Peptide Fragments - chemistry Peptide Fragments - isolation & purification Plant Proteins - chemistry pollen Pollen - chemistry separation spectral analysis sugars Trees Trypsin Xylose - analysis |
title | Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen |
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