Carbamylation inhibits the ferroxidase activity of caeruloplasmin
The ferroxidase activity of caeruloplasmin (EC 1.16.3.1) is an important antioxidant defence mechanism in man. In chronic renal failure proteins become carbamylated as a result of reactions with urea-derived cyanate. We have therefore investigated the effects of carbamylation on the ferroxidase acti...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1995-09, Vol.214 (3), p.1073-1078 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1078 |
|---|---|
| container_issue | 3 |
| container_start_page | 1073 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 214 |
| creator | Roxborough, H E Millar, C A McEneny, J Young, I S |
| description | The ferroxidase activity of caeruloplasmin (EC 1.16.3.1) is an important antioxidant defence mechanism in man. In chronic renal failure proteins become carbamylated as a result of reactions with urea-derived cyanate. We have therefore investigated the effects of carbamylation on the ferroxidase activity of caeruloplasmin. Increasing degrees of carbamylation produce a progressive impairment of ferroxidase activity measured using o-dianisidine as substrate, and the ability of caeruloplasmin to load ferrous iron onto ovotransferrin is reduced. Carbamylation of caeruloplasmin may contribute to reduced antioxidant capacity in patients with renal failure. |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_77560576</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77560576</sourcerecordid><originalsourceid>FETCH-LOGICAL-p532-b40f0eb1bef8738ee8025c9bbc968cd3f514c87fd09b0cfbe6f76a68b751f6023</originalsourceid><addsrcrecordid>eNotj81KxDAYAHNQ1nX1EYScvBW-tE3SHpfiHyx42YO3kqRf2Eja1CQV-_YK9jSXYWCuyB4ARFG27OOG3Kb0CcBYLdod2UkuOWflnhw7FbUaV6-yCxN108VplxPNF6QWYww_blAJqTLZfbu80mCpURgXH2av0uimO3JtlU94v_FAzs9P5-61OL2_vHXHUzHzqix0DRZQM422kVWD2EDJTau1aUVjhspyVptG2gFaDcZqFFYKJRotObMCyupAHv-zcwxfC6bcjy4Z9F5NGJbUS8kFcCn-xIdNXPSIQz9HN6q49tty9QtE81Lz</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77560576</pqid></control><display><type>article</type><title>Carbamylation inhibits the ferroxidase activity of caeruloplasmin</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Roxborough, H E ; Millar, C A ; McEneny, J ; Young, I S</creator><creatorcontrib>Roxborough, H E ; Millar, C A ; McEneny, J ; Young, I S</creatorcontrib><description>The ferroxidase activity of caeruloplasmin (EC 1.16.3.1) is an important antioxidant defence mechanism in man. In chronic renal failure proteins become carbamylated as a result of reactions with urea-derived cyanate. We have therefore investigated the effects of carbamylation on the ferroxidase activity of caeruloplasmin. Increasing degrees of carbamylation produce a progressive impairment of ferroxidase activity measured using o-dianisidine as substrate, and the ability of caeruloplasmin to load ferrous iron onto ovotransferrin is reduced. Carbamylation of caeruloplasmin may contribute to reduced antioxidant capacity in patients with renal failure.</description><identifier>ISSN: 0006-291X</identifier><identifier>PMID: 7575512</identifier><language>eng</language><publisher>United States</publisher><subject>Ceruloplasmin - antagonists & inhibitors ; Ceruloplasmin - chemistry ; Ceruloplasmin - metabolism ; Conalbumin - metabolism ; Cyanates - metabolism ; Cyanates - pharmacology ; Humans ; Iron - metabolism ; Kidney Failure, Chronic - enzymology ; Kinetics ; Time Factors</subject><ispartof>Biochemical and biophysical research communications, 1995-09, Vol.214 (3), p.1073-1078</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7575512$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roxborough, H E</creatorcontrib><creatorcontrib>Millar, C A</creatorcontrib><creatorcontrib>McEneny, J</creatorcontrib><creatorcontrib>Young, I S</creatorcontrib><title>Carbamylation inhibits the ferroxidase activity of caeruloplasmin</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The ferroxidase activity of caeruloplasmin (EC 1.16.3.1) is an important antioxidant defence mechanism in man. In chronic renal failure proteins become carbamylated as a result of reactions with urea-derived cyanate. We have therefore investigated the effects of carbamylation on the ferroxidase activity of caeruloplasmin. Increasing degrees of carbamylation produce a progressive impairment of ferroxidase activity measured using o-dianisidine as substrate, and the ability of caeruloplasmin to load ferrous iron onto ovotransferrin is reduced. Carbamylation of caeruloplasmin may contribute to reduced antioxidant capacity in patients with renal failure.</description><subject>Ceruloplasmin - antagonists & inhibitors</subject><subject>Ceruloplasmin - chemistry</subject><subject>Ceruloplasmin - metabolism</subject><subject>Conalbumin - metabolism</subject><subject>Cyanates - metabolism</subject><subject>Cyanates - pharmacology</subject><subject>Humans</subject><subject>Iron - metabolism</subject><subject>Kidney Failure, Chronic - enzymology</subject><subject>Kinetics</subject><subject>Time Factors</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotj81KxDAYAHNQ1nX1EYScvBW-tE3SHpfiHyx42YO3kqRf2Eja1CQV-_YK9jSXYWCuyB4ARFG27OOG3Kb0CcBYLdod2UkuOWflnhw7FbUaV6-yCxN108VplxPNF6QWYww_blAJqTLZfbu80mCpURgXH2av0uimO3JtlU94v_FAzs9P5-61OL2_vHXHUzHzqix0DRZQM422kVWD2EDJTau1aUVjhspyVptG2gFaDcZqFFYKJRotObMCyupAHv-zcwxfC6bcjy4Z9F5NGJbUS8kFcCn-xIdNXPSIQz9HN6q49tty9QtE81Lz</recordid><startdate>19950925</startdate><enddate>19950925</enddate><creator>Roxborough, H E</creator><creator>Millar, C A</creator><creator>McEneny, J</creator><creator>Young, I S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19950925</creationdate><title>Carbamylation inhibits the ferroxidase activity of caeruloplasmin</title><author>Roxborough, H E ; Millar, C A ; McEneny, J ; Young, I S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p532-b40f0eb1bef8738ee8025c9bbc968cd3f514c87fd09b0cfbe6f76a68b751f6023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Ceruloplasmin - antagonists & inhibitors</topic><topic>Ceruloplasmin - chemistry</topic><topic>Ceruloplasmin - metabolism</topic><topic>Conalbumin - metabolism</topic><topic>Cyanates - metabolism</topic><topic>Cyanates - pharmacology</topic><topic>Humans</topic><topic>Iron - metabolism</topic><topic>Kidney Failure, Chronic - enzymology</topic><topic>Kinetics</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roxborough, H E</creatorcontrib><creatorcontrib>Millar, C A</creatorcontrib><creatorcontrib>McEneny, J</creatorcontrib><creatorcontrib>Young, I S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roxborough, H E</au><au>Millar, C A</au><au>McEneny, J</au><au>Young, I S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbamylation inhibits the ferroxidase activity of caeruloplasmin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1995-09-25</date><risdate>1995</risdate><volume>214</volume><issue>3</issue><spage>1073</spage><epage>1078</epage><pages>1073-1078</pages><issn>0006-291X</issn><abstract>The ferroxidase activity of caeruloplasmin (EC 1.16.3.1) is an important antioxidant defence mechanism in man. In chronic renal failure proteins become carbamylated as a result of reactions with urea-derived cyanate. We have therefore investigated the effects of carbamylation on the ferroxidase activity of caeruloplasmin. Increasing degrees of carbamylation produce a progressive impairment of ferroxidase activity measured using o-dianisidine as substrate, and the ability of caeruloplasmin to load ferrous iron onto ovotransferrin is reduced. Carbamylation of caeruloplasmin may contribute to reduced antioxidant capacity in patients with renal failure.</abstract><cop>United States</cop><pmid>7575512</pmid><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1995-09, Vol.214 (3), p.1073-1078 |
| issn | 0006-291X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77560576 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Ceruloplasmin - antagonists & inhibitors Ceruloplasmin - chemistry Ceruloplasmin - metabolism Conalbumin - metabolism Cyanates - metabolism Cyanates - pharmacology Humans Iron - metabolism Kidney Failure, Chronic - enzymology Kinetics Time Factors |
| title | Carbamylation inhibits the ferroxidase activity of caeruloplasmin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T00%3A49%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Carbamylation%20inhibits%20the%20ferroxidase%20activity%20of%20caeruloplasmin&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Roxborough,%20H%20E&rft.date=1995-09-25&rft.volume=214&rft.issue=3&rft.spage=1073&rft.epage=1078&rft.pages=1073-1078&rft.issn=0006-291X&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E77560576%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77560576&rft_id=info:pmid/7575512&rfr_iscdi=true |