Specific cleavage of immunoglobulin G by copper ions
The hinge region of a recombinant‐DNA‐produced human IgG1 (Campath 1H) is specifically cleavable at a single copper‐sensitive peptide bond, yielding a distinct fragment resolved by size‐exclusion high‐performance liquid chromatography. This novel metal ion‐catalysed cleavage at slightly alkaline pH...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1996-07, Vol.48 (1), p.48-55 |
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| container_title | International Journal of Peptide and Protein Research |
| container_volume | 48 |
| creator | SMITH, MARJORIE A EASTON, MARK EVERETT, PETER LEWIS, GARNET PAYNE, MICHAEL RIVEROS-MORENO, VALENTINA ALLEN, GEOFFREY |
| description | The hinge region of a recombinant‐DNA‐produced human IgG1 (Campath 1H) is specifically cleavable at a single copper‐sensitive peptide bond, yielding a distinct fragment resolved by size‐exclusion high‐performance liquid chromatography. This novel metal ion‐catalysed cleavage at slightly alkaline pH is inhibited by EDTA and its rate is reduced at slightly acidic conditions (pH5‐6) and accelerated by increasing concentrations of cupric ion and higher temperature. Complete cleavage was observed after incubation at pH 8 for 24 h with 1 mM CuC12. Sequence analysis determined the cleavage site to be the Lys226‐Thr227 bond in the hinge‐region sequence DKTHT. Cleavage of other IgGs was observed to varying degrees, and specific cleavage of synthetic peptides containing this pentapeptide sequence was also observed. © Munksgaard 1996. |
| doi_str_mv | 10.1111/j.1399-3011.1996.tb01105.x |
| format | Article |
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This novel metal ion‐catalysed cleavage at slightly alkaline pH is inhibited by EDTA and its rate is reduced at slightly acidic conditions (pH5‐6) and accelerated by increasing concentrations of cupric ion and higher temperature. Complete cleavage was observed after incubation at pH 8 for 24 h with 1 mM CuC12. Sequence analysis determined the cleavage site to be the Lys226‐Thr227 bond in the hinge‐region sequence DKTHT. 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This novel metal ion‐catalysed cleavage at slightly alkaline pH is inhibited by EDTA and its rate is reduced at slightly acidic conditions (pH5‐6) and accelerated by increasing concentrations of cupric ion and higher temperature. Complete cleavage was observed after incubation at pH 8 for 24 h with 1 mM CuC12. Sequence analysis determined the cleavage site to be the Lys226‐Thr227 bond in the hinge‐region sequence DKTHT. Cleavage of other IgGs was observed to varying degrees, and specific cleavage of synthetic peptides containing this pentapeptide sequence was also observed. © Munksgaard 1996.</description><subject>Alemtuzumab</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Antibodies, Monoclonal, Humanized</subject><subject>Antibodies, Neoplasm - chemistry</subject><subject>Antibodies, Neoplasm - metabolism</subject><subject>Binding Sites</subject><subject>Campath</subject><subject>Cations</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>cleavage</subject><subject>copper</subject><subject>Copper - chemistry</subject><subject>Copper - metabolism</subject><subject>cupric ion</subject><subject>Edetic Acid - chemistry</subject><subject>hinge peptide</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>IgG</subject><subject>immunoglobulin G</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - metabolism</subject><subject>Metals - chemistry</subject><subject>Metals - metabolism</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Denaturation</subject><subject>Temperature</subject><subject>Time Factors</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE1PwkAQhjdGg4j-BJPGg7fWbafdDw8mCgpG1IMajpvudmoWW1q7VOHfWwLh7lx2knfmmc1DyEVIg7Crq3kQgpQ-0DAMQilZsNRdS5NgdUD6--iQ9Ckw7gvg_JicODenFGLgUY_0hIjjiEV9Er_VaGxujWcKTH_ST_Sq3LNl2S6qz6LSbWEX3tjTa89UdY2NZ6uFOyVHeVo4PNu9A_LxcP8-nPjT1_Hj8Hbqm5iD8Bl212TCZKpjoQ3niFSgzmiGiYE8YUCzrPu-ySHKQkZzAyJiPGbSaMi0gQG53HLrpvpu0S1VaZ3BokgXWLVOcQEyojLqBq-3g6apnGswV3Vjy7RZq5CqjTI1VxsvauNFbZSpnTK16pbPd1daXWK2X9056vKbbf5rC1z_g6yGd6NRLDqAvwVYt8TVHpA2X4px4ImavYzVMxtNnhKYKQ5_nF-J-g</recordid><startdate>199607</startdate><enddate>199607</enddate><creator>SMITH, MARJORIE A</creator><creator>EASTON, MARK</creator><creator>EVERETT, PETER</creator><creator>LEWIS, GARNET</creator><creator>PAYNE, MICHAEL</creator><creator>RIVEROS-MORENO, VALENTINA</creator><creator>ALLEN, GEOFFREY</creator><general>Blackwell Publishing Ltd</general><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>199607</creationdate><title>Specific cleavage of immunoglobulin G by copper ions</title><author>SMITH, MARJORIE A ; EASTON, MARK ; EVERETT, PETER ; LEWIS, GARNET ; PAYNE, MICHAEL ; RIVEROS-MORENO, VALENTINA ; ALLEN, GEOFFREY</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4738-6e4379569ab48bc77ee08ebd0de5c3f5630dd996cf32d160fc38267469cb3dbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Alemtuzumab</topic><topic>Antibodies, Monoclonal - chemistry</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Antibodies, Monoclonal, Humanized</topic><topic>Antibodies, Neoplasm - chemistry</topic><topic>Antibodies, Neoplasm - metabolism</topic><topic>Binding Sites</topic><topic>Campath</topic><topic>Cations</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>cleavage</topic><topic>copper</topic><topic>Copper - chemistry</topic><topic>Copper - metabolism</topic><topic>cupric ion</topic><topic>Edetic Acid - chemistry</topic><topic>hinge peptide</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>IgG</topic><topic>immunoglobulin G</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - metabolism</topic><topic>Metals - chemistry</topic><topic>Metals - metabolism</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Denaturation</topic><topic>Temperature</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SMITH, MARJORIE A</creatorcontrib><creatorcontrib>EASTON, MARK</creatorcontrib><creatorcontrib>EVERETT, PETER</creatorcontrib><creatorcontrib>LEWIS, GARNET</creatorcontrib><creatorcontrib>PAYNE, MICHAEL</creatorcontrib><creatorcontrib>RIVEROS-MORENO, VALENTINA</creatorcontrib><creatorcontrib>ALLEN, GEOFFREY</creatorcontrib><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>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SMITH, MARJORIE A</au><au>EASTON, MARK</au><au>EVERETT, PETER</au><au>LEWIS, GARNET</au><au>PAYNE, MICHAEL</au><au>RIVEROS-MORENO, VALENTINA</au><au>ALLEN, GEOFFREY</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific cleavage of immunoglobulin G by copper ions</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1996-07</date><risdate>1996</risdate><volume>48</volume><issue>1</issue><spage>48</spage><epage>55</epage><pages>48-55</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>The hinge region of a recombinant‐DNA‐produced human IgG1 (Campath 1H) is specifically cleavable at a single copper‐sensitive peptide bond, yielding a distinct fragment resolved by size‐exclusion high‐performance liquid chromatography. This novel metal ion‐catalysed cleavage at slightly alkaline pH is inhibited by EDTA and its rate is reduced at slightly acidic conditions (pH5‐6) and accelerated by increasing concentrations of cupric ion and higher temperature. Complete cleavage was observed after incubation at pH 8 for 24 h with 1 mM CuC12. Sequence analysis determined the cleavage site to be the Lys226‐Thr227 bond in the hinge‐region sequence DKTHT. Cleavage of other IgGs was observed to varying degrees, and specific cleavage of synthetic peptides containing this pentapeptide sequence was also observed. © Munksgaard 1996.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8844262</pmid><doi>10.1111/j.1399-3011.1996.tb01105.x</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| subjects | Alemtuzumab Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - metabolism Antibodies, Monoclonal, Humanized Antibodies, Neoplasm - chemistry Antibodies, Neoplasm - metabolism Binding Sites Campath Cations Chromatography, High Pressure Liquid - methods cleavage copper Copper - chemistry Copper - metabolism cupric ion Edetic Acid - chemistry hinge peptide Humans Hydrogen-Ion Concentration IgG immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - metabolism Metals - chemistry Metals - metabolism Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Denaturation Temperature Time Factors |
| title | Specific cleavage of immunoglobulin G by copper ions |
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