Comparative Analysis of Different Hemoglobins: Autoxidation, Reaction with Peroxide, and Lipid Oxidation
Beef hemoglobin (Hb) had lower levels of deoxyHb and autoxidized much slower as compared to trout Hb at pH 6.3. Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactiv...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2003-06, Vol.51 (13), p.3886-3891 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Richards, Mark P Dettmann, Mark A |
| description | Beef hemoglobin (Hb) had lower levels of deoxyHb and autoxidized much slower as compared to trout Hb at pH 6.3. Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactive with hydrogen peroxide. The autoxidation rate of perch Hb was more rapid than trout Hb despite the low deoxyHb content of perch Hb. Perch Hb was a better catalyst of lipid oxidation than trout Hb when added to washed cod muscle based on formation of lipid hydroperoxides and thiobarbituric acid reactive substances. These studies indicate that autoxidation rate does not always increase with increasing deoxyHb content. The role of heme crevice volume in heme protein autoxidation is discussed. Among other factors, these studies suggest that rates of lipid oxidation in various muscle foods may depend on the relative ability of hemoglobins from different animal species to promote lipid oxidation. Keywords: Trout; perch; chicken; beef; rancidity; blood; oxygen affinity; quality deterioration; muscle foods; Bohr effect; hydrogen peroxide; deoxyhemoglobin |
| doi_str_mv | 10.1021/jf0212082 |
| format | Article |
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Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactive with hydrogen peroxide. The autoxidation rate of perch Hb was more rapid than trout Hb despite the low deoxyHb content of perch Hb. Perch Hb was a better catalyst of lipid oxidation than trout Hb when added to washed cod muscle based on formation of lipid hydroperoxides and thiobarbituric acid reactive substances. These studies indicate that autoxidation rate does not always increase with increasing deoxyHb content. The role of heme crevice volume in heme protein autoxidation is discussed. Among other factors, these studies suggest that rates of lipid oxidation in various muscle foods may depend on the relative ability of hemoglobins from different animal species to promote lipid oxidation. Keywords: Trout; perch; chicken; beef; rancidity; blood; oxygen affinity; quality deterioration; muscle foods; Bohr effect; hydrogen peroxide; deoxyhemoglobin</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf0212082</identifier><identifier>PMID: 12797760</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>animal-based foods ; Animals ; autoxidation ; beef ; Biological and medical sciences ; Cattle - blood ; chickens ; Chickens - blood ; Fish and seafood industries ; Food industries ; Fundamental and applied biological sciences. Psychology ; heme ; hemoglobin ; Hemoglobins - analysis ; Hemoglobins - chemistry ; hydrogen peroxide ; Hydrogen-Ion Concentration ; hydroperoxides ; Lipid Peroxidation ; Meat and meat product industries ; Oncorhynchus mykiss - blood ; Oxidation-Reduction ; perch ; Perches - blood ; Peroxides - chemistry ; Species Specificity ; thiobarbituric acid-reactive substances ; trout</subject><ispartof>Journal of agricultural and food chemistry, 2003-06, Vol.51 (13), p.3886-3891</ispartof><rights>Copyright © 2003 American Chemical Society</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a403t-9c07b7a35e75b9b42655b88829f9a60655bfaf1834e78b55bd48e0573e21793b3</citedby><cites>FETCH-LOGICAL-a403t-9c07b7a35e75b9b42655b88829f9a60655bfaf1834e78b55bd48e0573e21793b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf0212082$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf0212082$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14882176$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12797760$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richards, Mark P</creatorcontrib><creatorcontrib>Dettmann, Mark A</creatorcontrib><title>Comparative Analysis of Different Hemoglobins: Autoxidation, Reaction with Peroxide, and Lipid Oxidation</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Beef hemoglobin (Hb) had lower levels of deoxyHb and autoxidized much slower as compared to trout Hb at pH 6.3. Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactive with hydrogen peroxide. The autoxidation rate of perch Hb was more rapid than trout Hb despite the low deoxyHb content of perch Hb. Perch Hb was a better catalyst of lipid oxidation than trout Hb when added to washed cod muscle based on formation of lipid hydroperoxides and thiobarbituric acid reactive substances. These studies indicate that autoxidation rate does not always increase with increasing deoxyHb content. The role of heme crevice volume in heme protein autoxidation is discussed. Among other factors, these studies suggest that rates of lipid oxidation in various muscle foods may depend on the relative ability of hemoglobins from different animal species to promote lipid oxidation. Keywords: Trout; perch; chicken; beef; rancidity; blood; oxygen affinity; quality deterioration; muscle foods; Bohr effect; hydrogen peroxide; deoxyhemoglobin</description><subject>animal-based foods</subject><subject>Animals</subject><subject>autoxidation</subject><subject>beef</subject><subject>Biological and medical sciences</subject><subject>Cattle - blood</subject><subject>chickens</subject><subject>Chickens - blood</subject><subject>Fish and seafood industries</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>heme</subject><subject>hemoglobin</subject><subject>Hemoglobins - analysis</subject><subject>Hemoglobins - chemistry</subject><subject>hydrogen peroxide</subject><subject>Hydrogen-Ion Concentration</subject><subject>hydroperoxides</subject><subject>Lipid Peroxidation</subject><subject>Meat and meat product industries</subject><subject>Oncorhynchus mykiss - blood</subject><subject>Oxidation-Reduction</subject><subject>perch</subject><subject>Perches - blood</subject><subject>Peroxides - chemistry</subject><subject>Species Specificity</subject><subject>thiobarbituric acid-reactive substances</subject><subject>trout</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkU1v1DAQhi0EokvhwB8AX0BCasAfcexwWy2wRYrUVT8uXKxJYhdvk3hrJ9DeuPI3-SV4tUv3wsXjmXn8WvMOQi8peU8Jox_WNp2MKPYIzahgJBOUqsdoRlI5U6KgR-hZjGtCiBKSPEVHlMlSyoLM0M3C9xsIMLofBs8H6O6ji9hb_MlZa4IZRnxqen_d-doN8eOfX7_xfBr9nWvTEz-c4HMDzfaGf7rxO16ZsO2ZEwxDiyu3cS0--wc_R08sdNG82MdjdPXl8-XiNKvOll8X8yqDnPAxKxsiawlcGCnqss5ZIUStlGKlLaEg28yCpYrnRqo6ZW2uDBGSG0ZlyWt-jN7udDfB304mjrp3sTFdB4PxU9SSc0WTEwl8twOb4GMMxupNcD2Ee02J3jqrH5xN7Ku96FT3pj2QeysT8GYPQGygswGGxsUDl6cJqCwSl-04F0dz99CHcKMLyaXQl6sLLc6r5bdltdKrxL_e8Ra8huuQNK8uGKE5IWnLeSEPP0MT9dpPIa0x_meEv2tNpM0</recordid><startdate>20030618</startdate><enddate>20030618</enddate><creator>Richards, Mark P</creator><creator>Dettmann, Mark A</creator><general>American Chemical Society</general><scope>FBQ</scope><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>7X8</scope></search><sort><creationdate>20030618</creationdate><title>Comparative Analysis of Different Hemoglobins: Autoxidation, Reaction with Peroxide, and Lipid Oxidation</title><author>Richards, Mark P ; Dettmann, Mark A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a403t-9c07b7a35e75b9b42655b88829f9a60655bfaf1834e78b55bd48e0573e21793b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>animal-based foods</topic><topic>Animals</topic><topic>autoxidation</topic><topic>beef</topic><topic>Biological and medical sciences</topic><topic>Cattle - blood</topic><topic>chickens</topic><topic>Chickens - blood</topic><topic>Fish and seafood industries</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>heme</topic><topic>hemoglobin</topic><topic>Hemoglobins - analysis</topic><topic>Hemoglobins - chemistry</topic><topic>hydrogen peroxide</topic><topic>Hydrogen-Ion Concentration</topic><topic>hydroperoxides</topic><topic>Lipid Peroxidation</topic><topic>Meat and meat product industries</topic><topic>Oncorhynchus mykiss - blood</topic><topic>Oxidation-Reduction</topic><topic>perch</topic><topic>Perches - blood</topic><topic>Peroxides - chemistry</topic><topic>Species Specificity</topic><topic>thiobarbituric acid-reactive substances</topic><topic>trout</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Richards, Mark P</creatorcontrib><creatorcontrib>Dettmann, Mark A</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Richards, Mark P</au><au>Dettmann, Mark A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Analysis of Different Hemoglobins: Autoxidation, Reaction with Peroxide, and Lipid Oxidation</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2003-06-18</date><risdate>2003</risdate><volume>51</volume><issue>13</issue><spage>3886</spage><epage>3891</epage><pages>3886-3891</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Beef hemoglobin (Hb) had lower levels of deoxyHb and autoxidized much slower as compared to trout Hb at pH 6.3. Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactive with hydrogen peroxide. The autoxidation rate of perch Hb was more rapid than trout Hb despite the low deoxyHb content of perch Hb. Perch Hb was a better catalyst of lipid oxidation than trout Hb when added to washed cod muscle based on formation of lipid hydroperoxides and thiobarbituric acid reactive substances. These studies indicate that autoxidation rate does not always increase with increasing deoxyHb content. The role of heme crevice volume in heme protein autoxidation is discussed. Among other factors, these studies suggest that rates of lipid oxidation in various muscle foods may depend on the relative ability of hemoglobins from different animal species to promote lipid oxidation. Keywords: Trout; perch; chicken; beef; rancidity; blood; oxygen affinity; quality deterioration; muscle foods; Bohr effect; hydrogen peroxide; deoxyhemoglobin</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12797760</pmid><doi>10.1021/jf0212082</doi><tpages>6</tpages></addata></record> |
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| subjects | animal-based foods Animals autoxidation beef Biological and medical sciences Cattle - blood chickens Chickens - blood Fish and seafood industries Food industries Fundamental and applied biological sciences. Psychology heme hemoglobin Hemoglobins - analysis Hemoglobins - chemistry hydrogen peroxide Hydrogen-Ion Concentration hydroperoxides Lipid Peroxidation Meat and meat product industries Oncorhynchus mykiss - blood Oxidation-Reduction perch Perches - blood Peroxides - chemistry Species Specificity thiobarbituric acid-reactive substances trout |
| title | Comparative Analysis of Different Hemoglobins: Autoxidation, Reaction with Peroxide, and Lipid Oxidation |
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