Recovery of the oxidative activity of caged bovine haemoglobin after UV photolysis
Caging of bovine haemoglobin with increasing amounts of 1-(2-nitrophenyl)ethyl (NPE) and uncaging after a 366 nm irradiation was examined. Caged and photolysed conjugates were characterised by enzymatic assay of the ABTS oxidation, UV/Vis absorbance, and electrospray mass ionisation. Modification of...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2004-07, Vol.320 (3), p.939-944 |
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| creator | Bédouet, Laurent Adenier, Hervé Pulvin, Sylviane Bedel-Cloutour, Catherine Thomas, Daniel |
| description | Caging of bovine haemoglobin with increasing amounts of 1-(2-nitrophenyl)ethyl (NPE) and uncaging after a 366
nm irradiation was examined. Caged and photolysed conjugates were characterised by enzymatic assay of the ABTS oxidation, UV/Vis absorbance, and electrospray mass ionisation. Modification of haemoglobin with 50, 75, and 100 equivalents of 1-(2-nitrophenyl)diazoethane led to a progressive decrease of enzymatic activity. Photolysis at 366
nm during 5, 15, and 30
min induced the recovery of a part of the enzymatic activity. ESI analyses showed that a reversible binding of up to 6 NPE groups per α-chain and that the removal of most of the photolabile groups occurred rapidly after 5
min of illumination at 366
nm and reached near completion after 15
min. A variable alteration of haemoglobin after labelling could explain that the complete removal of NPE groups did not restore its full oxidative activity. |
| doi_str_mv | 10.1016/j.bbrc.2004.06.043 |
| format | Article |
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nm irradiation was examined. Caged and photolysed conjugates were characterised by enzymatic assay of the ABTS oxidation, UV/Vis absorbance, and electrospray mass ionisation. Modification of haemoglobin with 50, 75, and 100 equivalents of 1-(2-nitrophenyl)diazoethane led to a progressive decrease of enzymatic activity. Photolysis at 366
nm during 5, 15, and 30
min induced the recovery of a part of the enzymatic activity. ESI analyses showed that a reversible binding of up to 6 NPE groups per α-chain and that the removal of most of the photolabile groups occurred rapidly after 5
min of illumination at 366
nm and reached near completion after 15
min. A variable alteration of haemoglobin after labelling could explain that the complete removal of NPE groups did not restore its full oxidative activity.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2004.06.043</identifier><identifier>PMID: 15240139</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Azo Compounds - chemistry ; Azo Compounds - metabolism ; Caged haemoglobin ; Cattle ; Chemical modification ; Enzyme Activation - radiation effects ; Enzyme Reactivators - chemistry ; Enzyme Reactivators - radiation effects ; Hemoglobins - chemistry ; Hemoglobins - radiation effects ; Hemoprotein ; Inactivation ; Kinetics ; Nitrobenzenes - chemistry ; Nitrobenzenes - metabolism ; Oxidation-Reduction ; Photochemistry - methods ; Photolysis ; Photolysis - radiation effects ; Protein Binding - radiation effects ; Ultraviolet Rays</subject><ispartof>Biochemical and biophysical research communications, 2004-07, Vol.320 (3), p.939-944</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-2e1cbce1ce50afeff6783b91ede5ded04a0dced1af734e34920563e121affc8d3</citedby><cites>FETCH-LOGICAL-c381t-2e1cbce1ce50afeff6783b91ede5ded04a0dced1af734e34920563e121affc8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X04012690$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15240139$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bédouet, Laurent</creatorcontrib><creatorcontrib>Adenier, Hervé</creatorcontrib><creatorcontrib>Pulvin, Sylviane</creatorcontrib><creatorcontrib>Bedel-Cloutour, Catherine</creatorcontrib><creatorcontrib>Thomas, Daniel</creatorcontrib><title>Recovery of the oxidative activity of caged bovine haemoglobin after UV photolysis</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Caging of bovine haemoglobin with increasing amounts of 1-(2-nitrophenyl)ethyl (NPE) and uncaging after a 366
nm irradiation was examined. Caged and photolysed conjugates were characterised by enzymatic assay of the ABTS oxidation, UV/Vis absorbance, and electrospray mass ionisation. Modification of haemoglobin with 50, 75, and 100 equivalents of 1-(2-nitrophenyl)diazoethane led to a progressive decrease of enzymatic activity. Photolysis at 366
nm during 5, 15, and 30
min induced the recovery of a part of the enzymatic activity. ESI analyses showed that a reversible binding of up to 6 NPE groups per α-chain and that the removal of most of the photolabile groups occurred rapidly after 5
min of illumination at 366
nm and reached near completion after 15
min. A variable alteration of haemoglobin after labelling could explain that the complete removal of NPE groups did not restore its full oxidative activity.</description><subject>Animals</subject><subject>Azo Compounds - chemistry</subject><subject>Azo Compounds - metabolism</subject><subject>Caged haemoglobin</subject><subject>Cattle</subject><subject>Chemical modification</subject><subject>Enzyme Activation - radiation effects</subject><subject>Enzyme Reactivators - chemistry</subject><subject>Enzyme Reactivators - radiation effects</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - radiation effects</subject><subject>Hemoprotein</subject><subject>Inactivation</subject><subject>Kinetics</subject><subject>Nitrobenzenes - chemistry</subject><subject>Nitrobenzenes - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Photochemistry - methods</subject><subject>Photolysis</subject><subject>Photolysis - radiation effects</subject><subject>Protein Binding - radiation effects</subject><subject>Ultraviolet Rays</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9LAzEQxYMotla_gAfJyduuk8027YIXKf6DglCseAvZZNKmbJuabIv99qa24M3LPJh585j5EXLNIGfAxN0ir-ug8wKgzEHkUPIT0mVQQVYwKE9JFwBEVlTss0MuYlwAMFaK6px0WL8ogfGqSyYT1H6LYUe9pe0cqf92RrVui1TpJK79nWg1Q0Nrv3UrpHOFSz9rfO1WVNkWA51-0PXct77ZRRcvyZlVTcSro_bI9OnxffSSjd-eX0cP40zzIWuzApmudSrYB2XRWjEY8rpiaLBv0ECpwGg0TNkBL5GXVQF9wZEVqWP10PAeuT3kroP_2mBs5dJFjU2jVug3UQohhlxwSMbiYNTBxxjQynVwSxV2koHck5QLuScp9yQlCJlIpqWbY_qmXqL5WzmiS4b7gwHTj1uHQUbtcJVOdgF1K413_-X_AGw4hqE</recordid><startdate>20040730</startdate><enddate>20040730</enddate><creator>Bédouet, Laurent</creator><creator>Adenier, Hervé</creator><creator>Pulvin, Sylviane</creator><creator>Bedel-Cloutour, Catherine</creator><creator>Thomas, Daniel</creator><general>Elsevier Inc</general><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>20040730</creationdate><title>Recovery of the oxidative activity of caged bovine haemoglobin after UV photolysis</title><author>Bédouet, Laurent ; Adenier, Hervé ; Pulvin, Sylviane ; Bedel-Cloutour, Catherine ; Thomas, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-2e1cbce1ce50afeff6783b91ede5ded04a0dced1af734e34920563e121affc8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Azo Compounds - chemistry</topic><topic>Azo Compounds - metabolism</topic><topic>Caged haemoglobin</topic><topic>Cattle</topic><topic>Chemical modification</topic><topic>Enzyme Activation - radiation effects</topic><topic>Enzyme Reactivators - chemistry</topic><topic>Enzyme Reactivators - radiation effects</topic><topic>Hemoglobins - chemistry</topic><topic>Hemoglobins - radiation effects</topic><topic>Hemoprotein</topic><topic>Inactivation</topic><topic>Kinetics</topic><topic>Nitrobenzenes - chemistry</topic><topic>Nitrobenzenes - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Photochemistry - methods</topic><topic>Photolysis</topic><topic>Photolysis - radiation effects</topic><topic>Protein Binding - radiation effects</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bédouet, Laurent</creatorcontrib><creatorcontrib>Adenier, Hervé</creatorcontrib><creatorcontrib>Pulvin, Sylviane</creatorcontrib><creatorcontrib>Bedel-Cloutour, Catherine</creatorcontrib><creatorcontrib>Thomas, Daniel</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bédouet, Laurent</au><au>Adenier, Hervé</au><au>Pulvin, Sylviane</au><au>Bedel-Cloutour, Catherine</au><au>Thomas, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recovery of the oxidative activity of caged bovine haemoglobin after UV photolysis</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-07-30</date><risdate>2004</risdate><volume>320</volume><issue>3</issue><spage>939</spage><epage>944</epage><pages>939-944</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Caging of bovine haemoglobin with increasing amounts of 1-(2-nitrophenyl)ethyl (NPE) and uncaging after a 366
nm irradiation was examined. Caged and photolysed conjugates were characterised by enzymatic assay of the ABTS oxidation, UV/Vis absorbance, and electrospray mass ionisation. Modification of haemoglobin with 50, 75, and 100 equivalents of 1-(2-nitrophenyl)diazoethane led to a progressive decrease of enzymatic activity. Photolysis at 366
nm during 5, 15, and 30
min induced the recovery of a part of the enzymatic activity. ESI analyses showed that a reversible binding of up to 6 NPE groups per α-chain and that the removal of most of the photolabile groups occurred rapidly after 5
min of illumination at 366
nm and reached near completion after 15
min. A variable alteration of haemoglobin after labelling could explain that the complete removal of NPE groups did not restore its full oxidative activity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15240139</pmid><doi>10.1016/j.bbrc.2004.06.043</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Azo Compounds - chemistry Azo Compounds - metabolism Caged haemoglobin Cattle Chemical modification Enzyme Activation - radiation effects Enzyme Reactivators - chemistry Enzyme Reactivators - radiation effects Hemoglobins - chemistry Hemoglobins - radiation effects Hemoprotein Inactivation Kinetics Nitrobenzenes - chemistry Nitrobenzenes - metabolism Oxidation-Reduction Photochemistry - methods Photolysis Photolysis - radiation effects Protein Binding - radiation effects Ultraviolet Rays |
| title | Recovery of the oxidative activity of caged bovine haemoglobin after UV photolysis |
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