The glycopeptides of the mouse immunoglobulin A T15
Cleavage of mouse IgA T15 with papain yielded (a) a glycosylated Fab fragment, (b) a non-glycosylated Fc fragment and (c) a glycosylated C-terminal peptide. The cleavage sites at the hinge and at the end of the Cα3 domain were located by sequencing. The two glycopeptides were prepared from the Fab a...
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| Veröffentlicht in: | Molecular immunology 1990-11, Vol.27 (11), p.1083-1090 |
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| container_title | Molecular immunology |
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| creator | Young, N.Martin Jackson, Gail E.D. Brisson, Jean-Robert |
| description | Cleavage of mouse IgA T15 with papain yielded (a) a glycosylated Fab fragment, (b) a non-glycosylated Fc fragment and (c) a glycosylated C-terminal peptide. The cleavage sites at the hinge and at the end of the Cα3 domain were located by sequencing. The two glycopeptides were prepared from the Fab and C-terminal fragments by pronase digestion. The Cα1 glycopeptide at Asn 155 was complex type with α(1–3)galactose terminal groups, and closely resembled the Asn 171 glycopeptide of mouse IgM (Anderson
et al. (1985)
Arch. Biochem. Biophys.
243, 605–618). In contrast, the C-terminal glycopeptide at Asn 446 was entirely different from the corresponding IgM glycopeptide, being complex rather than high-mannose type. |
| doi_str_mv | 10.1016/0161-5890(90)90096-I |
| format | Article |
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et al. (1985)
Arch. Biochem. Biophys.
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et al. (1985)
Arch. Biochem. Biophys.
243, 605–618). In contrast, the C-terminal glycopeptide at Asn 446 was entirely different from the corresponding IgM glycopeptide, being complex rather than high-mannose type.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Antibodies, immunoglobulins</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Sequence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Glycopeptides - chemistry</subject><subject>Glycosylation</subject><subject>Immunoglobulin A - chemistry</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Mice</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Papain</subject><subject>Pepsin A</subject><subject>Peptide Fragments</subject><subject>Structure</subject><subject>Structure-Activity Relationship</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAQgIMouj7-gUIPInqozqRJmlwEER8Lgpe9hzSdaqSPtWkF_71dd9mjQobAzDcPPsZOEa4RUN1MganUBi4NXBkAo9L5DpuhznlqUPBdNtsiB-wwxg8AUKDkPtvnXOSg8xnLFu-UvNXfvlvScgglxaSrkmFKNt0YKQlNM7bdW90VYx3a5C5ZoDxme5WrI51s_iO2eHxY3D-nL69P8_u7l9QLzIdUepd5LUi6wqPOCqELAskzNBV3gpc5oZIu18ah4o4XruCi0EYDz4REnh2xi_XYZd99jhQH24Toqa5dS9NtVgMKobj6F0QFmcQMJ1CsQd93MfZU2WUfGtd_WwS7cmpXwuxKmP19k1M7n9rONvPHoqFy27SRONXPN3UXvaur3rU-xC0mFaARq-23a4wmZ1-Beht9oNZTGXrygy278PcdP36pj8Y</recordid><startdate>19901101</startdate><enddate>19901101</enddate><creator>Young, N.Martin</creator><creator>Jackson, Gail E.D.</creator><creator>Brisson, Jean-Robert</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19901101</creationdate><title>The glycopeptides of the mouse immunoglobulin A T15</title><author>Young, N.Martin ; Jackson, Gail E.D. ; Brisson, Jean-Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-5ca3c84e5abc183b48be052319f2a42d7e165a789a162a2bab24b89802345123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Antibodies, immunoglobulins</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Sequence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Glycopeptides - chemistry</topic><topic>Glycosylation</topic><topic>Immunoglobulin A - chemistry</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Mice</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Papain</topic><topic>Pepsin A</topic><topic>Peptide Fragments</topic><topic>Structure</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Young, N.Martin</creatorcontrib><creatorcontrib>Jackson, Gail E.D.</creatorcontrib><creatorcontrib>Brisson, Jean-Robert</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Young, N.Martin</au><au>Jackson, Gail E.D.</au><au>Brisson, Jean-Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The glycopeptides of the mouse immunoglobulin A T15</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>1990-11-01</date><risdate>1990</risdate><volume>27</volume><issue>11</issue><spage>1083</spage><epage>1090</epage><pages>1083-1090</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><coden>MOIMD5</coden><abstract>Cleavage of mouse IgA T15 with papain yielded (a) a glycosylated Fab fragment, (b) a non-glycosylated Fc fragment and (c) a glycosylated C-terminal peptide. The cleavage sites at the hinge and at the end of the Cα3 domain were located by sequencing. The two glycopeptides were prepared from the Fab and C-terminal fragments by pronase digestion. The Cα1 glycopeptide at Asn 155 was complex type with α(1–3)galactose terminal groups, and closely resembled the Asn 171 glycopeptide of mouse IgM (Anderson
et al. (1985)
Arch. Biochem. Biophys.
243, 605–618). In contrast, the C-terminal glycopeptide at Asn 446 was entirely different from the corresponding IgM glycopeptide, being complex rather than high-mannose type.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>2247087</pmid><doi>10.1016/0161-5890(90)90096-I</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Molecular immunology, 1990-11, Vol.27 (11), p.1083-1090 |
| issn | 0161-5890 1872-9142 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Amino Acids - analysis Animals Antibodies, immunoglobulins Biological and medical sciences Carbohydrate Sequence Fundamental and applied biological sciences. Psychology Fundamental immunology Glycopeptides - chemistry Glycosylation Immunoglobulin A - chemistry Immunoglobulin Fab Fragments - chemistry Mice Molecular immunology Molecular Sequence Data Papain Pepsin A Peptide Fragments Structure Structure-Activity Relationship |
| title | The glycopeptides of the mouse immunoglobulin A T15 |
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