Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G
We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Analysis b...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1991-12, Vol.110 (6), p.868-872 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Zanma, Akira Matsumoto, Yoh-ichi Masuho, Yasuhiko |
| description | We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Analysis by gel filtration and SDS-PAGE revealed that the conjugates were composed of one molecule of SOD linked with one molecule of Fc [SOD-(Fc)1] and one SOD molecule linked with several Fc molecule [SOD-(Fc)n]. The resulting SOD-Fc conjugates retained more than 90% of the enzyme activity of SOD. When those conjugates were administered intravenously to mice, the half-lives of SOD activity in the circulation were 29 and 42 h for SOD-(Fc)1 and SOD-(Fc)n, respectively, while free SOD had a half-life of 5 min. Intravenous administration of the conjugates to mice markedly repressed the increase in serum glutamic-oxaloacetic transaminase (GOT) activity induced by paraquat. These results suggest that SOD-Fc conjugates, which have long half-lives, effectively perform dismutation of superoxide radicals and may be useful for preventing tissue injury caused by hazardous oxygen metabolites. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a123681 |
| format | Article |
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The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Analysis by gel filtration and SDS-PAGE revealed that the conjugates were composed of one molecule of SOD linked with one molecule of Fc [SOD-(Fc)1] and one SOD molecule linked with several Fc molecule [SOD-(Fc)n]. The resulting SOD-Fc conjugates retained more than 90% of the enzyme activity of SOD. When those conjugates were administered intravenously to mice, the half-lives of SOD activity in the circulation were 29 and 42 h for SOD-(Fc)1 and SOD-(Fc)n, respectively, while free SOD had a half-life of 5 min. Intravenous administration of the conjugates to mice markedly repressed the increase in serum glutamic-oxaloacetic transaminase (GOT) activity induced by paraquat. These results suggest that SOD-Fc conjugates, which have long half-lives, effectively perform dismutation of superoxide radicals and may be useful for preventing tissue injury caused by hazardous oxygen metabolites.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a123681</identifier><identifier>PMID: 1665488</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject><![CDATA[Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Half-Life ; Humans ; Immunoglobulin Fc Fragments - administration & dosage ; Immunoglobulin Fc Fragments - isolation & purification ; Immunoglobulin Fc Fragments - metabolism ; Immunoglobulin G - administration & dosage ; Immunoglobulin G - isolation & purification ; Immunoglobulin G - metabolism ; Mice ; Mice, Inbred ICR ; Oxidoreductases ; Paraquat - toxicity ; Superoxide Dismutase - administration & dosage ; Superoxide Dismutase - isolation & purification ; Superoxide Dismutase - pharmacokinetics ; Superoxides - metabolism]]></subject><ispartof>Journal of biochemistry (Tokyo), 1991-12, Vol.110 (6), p.868-872</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-c75e346997dea836d32c3c27f8987c78a9b7d5347d244bd8ee1b0d1514c4399a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5216433$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1665488$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zanma, Akira</creatorcontrib><creatorcontrib>Matsumoto, Yoh-ichi</creatorcontrib><creatorcontrib>Masuho, Yasuhiko</creatorcontrib><title>Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Analysis by gel filtration and SDS-PAGE revealed that the conjugates were composed of one molecule of SOD linked with one molecule of Fc [SOD-(Fc)1] and one SOD molecule linked with several Fc molecule [SOD-(Fc)n]. The resulting SOD-Fc conjugates retained more than 90% of the enzyme activity of SOD. When those conjugates were administered intravenously to mice, the half-lives of SOD activity in the circulation were 29 and 42 h for SOD-(Fc)1 and SOD-(Fc)n, respectively, while free SOD had a half-life of 5 min. Intravenous administration of the conjugates to mice markedly repressed the increase in serum glutamic-oxaloacetic transaminase (GOT) activity induced by paraquat. These results suggest that SOD-Fc conjugates, which have long half-lives, effectively perform dismutation of superoxide radicals and may be useful for preventing tissue injury caused by hazardous oxygen metabolites.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Half-Life</subject><subject>Humans</subject><subject>Immunoglobulin Fc Fragments - administration & dosage</subject><subject>Immunoglobulin Fc Fragments - isolation & purification</subject><subject>Immunoglobulin Fc Fragments - metabolism</subject><subject>Immunoglobulin G - administration & dosage</subject><subject>Immunoglobulin G - isolation & purification</subject><subject>Immunoglobulin G - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Oxidoreductases</subject><subject>Paraquat - toxicity</subject><subject>Superoxide Dismutase - administration & dosage</subject><subject>Superoxide Dismutase - isolation & purification</subject><subject>Superoxide Dismutase - pharmacokinetics</subject><subject>Superoxides - metabolism</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE2P0zAQhi0EWroLPwEpB-CWEnscOz5wQIXuLq3EYUGsuFiOPWlTkrhrx6L772mVahGn0eh95kMPIe9oMaeFgg_-0Pjgdj6FwXRxvqvtFvu5oQxERZ-RGZWlyJko6XMyKwpGc8X4_UtyGePu1DKAC3JBhSh5Vc3IauGHXdqYEWPmm-wu7TH4Q-sw-9zGPo0mYvanHbfZuMVsabNlMJseh_EE3_Z9Gvym83Xq2iG7fkVeNMeX8PW5XpEfyy_fFzf5-tv17eLTOrdc0jG3skTgQinp0FQgHDALlsmmUpW0sjKqlq4ELh3jvHYVIq0LR0vKLQelDFyR99PeffAPCeOo-zZa7DozoE9RU6EYMAlH8OME2uBjDNjofWh7Ex41LfRJpv5fpp5k6rPM4_yb86FU9-j-TU_2jvnbc26iNV0TzGDb-ISVjAoOpzfyCWvjiIen2ITfWkiQpb65_6UlrL4uV3dr_RP-ArXIlDY</recordid><startdate>19911201</startdate><enddate>19911201</enddate><creator>Zanma, Akira</creator><creator>Matsumoto, Yoh-ichi</creator><creator>Masuho, Yasuhiko</creator><general>Oxford University Press</general><scope>BSCLL</scope><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></search><sort><creationdate>19911201</creationdate><title>Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G</title><author>Zanma, Akira ; Matsumoto, Yoh-ichi ; Masuho, Yasuhiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-c75e346997dea836d32c3c27f8987c78a9b7d5347d244bd8ee1b0d1514c4399a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Half-Life</topic><topic>Humans</topic><topic>Immunoglobulin Fc Fragments - administration & dosage</topic><topic>Immunoglobulin Fc Fragments - isolation & purification</topic><topic>Immunoglobulin Fc Fragments - metabolism</topic><topic>Immunoglobulin G - administration & dosage</topic><topic>Immunoglobulin G - isolation & purification</topic><topic>Immunoglobulin G - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Oxidoreductases</topic><topic>Paraquat - toxicity</topic><topic>Superoxide Dismutase - administration & dosage</topic><topic>Superoxide Dismutase - isolation & purification</topic><topic>Superoxide Dismutase - pharmacokinetics</topic><topic>Superoxides - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zanma, Akira</creatorcontrib><creatorcontrib>Matsumoto, Yoh-ichi</creatorcontrib><creatorcontrib>Masuho, Yasuhiko</creatorcontrib><collection>Istex</collection><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><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zanma, Akira</au><au>Matsumoto, Yoh-ichi</au><au>Masuho, Yasuhiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1991-12-01</date><risdate>1991</risdate><volume>110</volume><issue>6</issue><spage>868</spage><epage>872</epage><pages>868-872</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Analysis by gel filtration and SDS-PAGE revealed that the conjugates were composed of one molecule of SOD linked with one molecule of Fc [SOD-(Fc)1] and one SOD molecule linked with several Fc molecule [SOD-(Fc)n]. The resulting SOD-Fc conjugates retained more than 90% of the enzyme activity of SOD. When those conjugates were administered intravenously to mice, the half-lives of SOD activity in the circulation were 29 and 42 h for SOD-(Fc)1 and SOD-(Fc)n, respectively, while free SOD had a half-life of 5 min. Intravenous administration of the conjugates to mice markedly repressed the increase in serum glutamic-oxaloacetic transaminase (GOT) activity induced by paraquat. These results suggest that SOD-Fc conjugates, which have long half-lives, effectively perform dismutation of superoxide radicals and may be useful for preventing tissue injury caused by hazardous oxygen metabolites.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>1665488</pmid><doi>10.1093/oxfordjournals.jbchem.a123681</doi><tpages>5</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Half-Life Humans Immunoglobulin Fc Fragments - administration & dosage Immunoglobulin Fc Fragments - isolation & purification Immunoglobulin Fc Fragments - metabolism Immunoglobulin G - administration & dosage Immunoglobulin G - isolation & purification Immunoglobulin G - metabolism Mice Mice, Inbred ICR Oxidoreductases Paraquat - toxicity Superoxide Dismutase - administration & dosage Superoxide Dismutase - isolation & purification Superoxide Dismutase - pharmacokinetics Superoxides - metabolism |
| title | Conjugates of Superoxide Dismutase with the Fc Fragment of Immunoglobulin G |
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