Species-specific effects on non-enzymatic metmyoglobin reduction in vitro
Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, an...
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| Veröffentlicht in: | Meat science 2015-07, Vol.105, p.108-113 |
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| creator | Elroy, N.N. Rogers, J. Mafi, G.G. VanOverbeke, D.L. Hartson, S.D. Ramanathan, R. |
| description | Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, and equine metmyoglobins (0.05mM) were reduced at pH5.6 and 7.4 in the presence or absence of HNE. Rates of metmyoglobin reduction were monitored by spectrophotometry, and myoglobin adducts were characterized by high-resolution mass-spectrometry. Results showed that the species origins of individual myoglobins determined rates of non-enzymatic reduction (beef>equine>pork; P |
| doi_str_mv | 10.1016/j.meatsci.2015.03.010 |
| format | Article |
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•Non-enzymatic metmyoglobin reduction is species-specific.•Number of histidine residues determines non-enzymatic metmyoglobin reduction.•pH5.6 resulted in greater metmyoglobin reduction compared with pH7.4.•Covalent binding of HNE decreased metmyoglobin reduction.</description><identifier>ISSN: 0309-1740</identifier><identifier>EISSN: 1873-4138</identifier><identifier>DOI: 10.1016/j.meatsci.2015.03.010</identifier><identifier>PMID: 25828165</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Aldehydes - pharmacology ; Animals ; Cattle ; Cross-Linking Reagents - pharmacology ; Dietary Proteins - chemistry ; Dietary Proteins - isolation & purification ; Dietary Proteins - metabolism ; Electron Transport - drug effects ; Horses ; Hydrogen-Ion Concentration ; Kinetics ; Lipid oxidation ; Lipid Peroxidation ; Mass spectrometry ; Meat color ; Metmyoglobin - chemistry ; Metmyoglobin - isolation & purification ; Metmyoglobin - metabolism ; Metmyoglobin reduction ; Models, Molecular ; Molecular Weight ; Myoglobin ; Oxidation-Reduction ; Pigments, Biological - chemistry ; Pigments, Biological - isolation & purification ; Pigments, Biological - metabolism ; Species Specificity ; Spectrometry, Mass, Electrospray Ionization ; Sus scrofa</subject><ispartof>Meat science, 2015-07, Vol.105, p.108-113</ispartof><rights>2015 Elsevier Ltd</rights><rights>Copyright © 2015 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c365t-8e8ce6c18645d2efd38350395a77911d9026986ca4bca7222d3cc86803ade3fe3</citedby><cites>FETCH-LOGICAL-c365t-8e8ce6c18645d2efd38350395a77911d9026986ca4bca7222d3cc86803ade3fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0309174015000716$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25828165$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Elroy, N.N.</creatorcontrib><creatorcontrib>Rogers, J.</creatorcontrib><creatorcontrib>Mafi, G.G.</creatorcontrib><creatorcontrib>VanOverbeke, D.L.</creatorcontrib><creatorcontrib>Hartson, S.D.</creatorcontrib><creatorcontrib>Ramanathan, R.</creatorcontrib><title>Species-specific effects on non-enzymatic metmyoglobin reduction in vitro</title><title>Meat science</title><addtitle>Meat Sci</addtitle><description>Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, and equine metmyoglobins (0.05mM) were reduced at pH5.6 and 7.4 in the presence or absence of HNE. Rates of metmyoglobin reduction were monitored by spectrophotometry, and myoglobin adducts were characterized by high-resolution mass-spectrometry. Results showed that the species origins of individual myoglobins determined rates of non-enzymatic reduction (beef>equine>pork; P<0.05). Irrespective of species, pre-incubation of HNE myoglobin decreased non-enzymatic metmyoglobin reduction compared with control at both pH5.6 and 7.4 (P<0.05). Mass spectrometric analysis revealed adducts of HNE with bovine, porcine, and equine myoglobins. The results indicate that the amino acid composition and the covalent binding of HNE with myoglobin can significantly decrease the ability of heme to accept electrons.
•Non-enzymatic metmyoglobin reduction is species-specific.•Number of histidine residues determines non-enzymatic metmyoglobin reduction.•pH5.6 resulted in greater metmyoglobin reduction compared with pH7.4.•Covalent binding of HNE decreased metmyoglobin reduction.</description><subject>Aldehydes - pharmacology</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cross-Linking Reagents - pharmacology</subject><subject>Dietary Proteins - chemistry</subject><subject>Dietary Proteins - isolation & purification</subject><subject>Dietary Proteins - metabolism</subject><subject>Electron Transport - drug effects</subject><subject>Horses</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Lipid oxidation</subject><subject>Lipid Peroxidation</subject><subject>Mass spectrometry</subject><subject>Meat color</subject><subject>Metmyoglobin - chemistry</subject><subject>Metmyoglobin - isolation & purification</subject><subject>Metmyoglobin - metabolism</subject><subject>Metmyoglobin reduction</subject><subject>Models, Molecular</subject><subject>Molecular Weight</subject><subject>Myoglobin</subject><subject>Oxidation-Reduction</subject><subject>Pigments, Biological - chemistry</subject><subject>Pigments, Biological - isolation & purification</subject><subject>Pigments, Biological - metabolism</subject><subject>Species Specificity</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Sus scrofa</subject><issn>0309-1740</issn><issn>1873-4138</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotlZ_gtKjl10nyW42exIpfhQKHtRzSJNZSeluarJbqL_elFavnoZhnneGeQi5ppBToOJulbeo-2hczoCWOfAcKJyQMZUVzwrK5SkZA4c6o1UBI3IR4woAKGfynIxYKZmkohyT-dsGjcOYxX1tnJli06Dp49R30853GXbfu1b3adBi3-7859ovXTcNaAfTuwSlZuv64C_JWaPXEa-OdUI-nh7fZy_Z4vV5PntYZIaLss8kSoPCUCmK0jJsLJe8BF6XuqpqSm0NTNRSGF0sja4YY5YbI4UEri3yBvmE3B72boL_GjD2qnXR4HqtO_RDVFRUBYOaF3VCywNqgo8xYKM2wbU67BQFtbeoVupoUe0tKuAqWUy5m-OJYdmi_Uv9akvA_QHA9OjWYVBpBXYGrQtJnrLe_XPiB2vlhkw</recordid><startdate>201507</startdate><enddate>201507</enddate><creator>Elroy, N.N.</creator><creator>Rogers, J.</creator><creator>Mafi, G.G.</creator><creator>VanOverbeke, D.L.</creator><creator>Hartson, S.D.</creator><creator>Ramanathan, R.</creator><general>Elsevier Ltd</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>201507</creationdate><title>Species-specific effects on non-enzymatic metmyoglobin reduction in vitro</title><author>Elroy, N.N. ; Rogers, J. ; Mafi, G.G. ; VanOverbeke, D.L. ; Hartson, S.D. ; Ramanathan, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c365t-8e8ce6c18645d2efd38350395a77911d9026986ca4bca7222d3cc86803ade3fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Aldehydes - pharmacology</topic><topic>Animals</topic><topic>Cattle</topic><topic>Cross-Linking Reagents - pharmacology</topic><topic>Dietary Proteins - chemistry</topic><topic>Dietary Proteins - isolation & purification</topic><topic>Dietary Proteins - metabolism</topic><topic>Electron Transport - drug effects</topic><topic>Horses</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lipid oxidation</topic><topic>Lipid Peroxidation</topic><topic>Mass spectrometry</topic><topic>Meat color</topic><topic>Metmyoglobin - chemistry</topic><topic>Metmyoglobin - isolation & purification</topic><topic>Metmyoglobin - metabolism</topic><topic>Metmyoglobin reduction</topic><topic>Models, Molecular</topic><topic>Molecular Weight</topic><topic>Myoglobin</topic><topic>Oxidation-Reduction</topic><topic>Pigments, Biological - chemistry</topic><topic>Pigments, Biological - isolation & purification</topic><topic>Pigments, Biological - metabolism</topic><topic>Species Specificity</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Sus scrofa</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Elroy, N.N.</creatorcontrib><creatorcontrib>Rogers, J.</creatorcontrib><creatorcontrib>Mafi, G.G.</creatorcontrib><creatorcontrib>VanOverbeke, D.L.</creatorcontrib><creatorcontrib>Hartson, S.D.</creatorcontrib><creatorcontrib>Ramanathan, R.</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>Meat science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Elroy, N.N.</au><au>Rogers, J.</au><au>Mafi, G.G.</au><au>VanOverbeke, D.L.</au><au>Hartson, S.D.</au><au>Ramanathan, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Species-specific effects on non-enzymatic metmyoglobin reduction in vitro</atitle><jtitle>Meat science</jtitle><addtitle>Meat Sci</addtitle><date>2015-07</date><risdate>2015</risdate><volume>105</volume><spage>108</spage><epage>113</epage><pages>108-113</pages><issn>0309-1740</issn><eissn>1873-4138</eissn><abstract>Our objectives were to determine the non-enzymatic metmyoglobin reduction properties of bovine, porcine, and equine myoglobins and to characterize the effects of pre-incubation of 4-hydroxy-2-nonenal (HNE) with myoglobins on non-enzymatic metmyoglobin reduction in vitro. Purified bovine, porcine, and equine metmyoglobins (0.05mM) were reduced at pH5.6 and 7.4 in the presence or absence of HNE. Rates of metmyoglobin reduction were monitored by spectrophotometry, and myoglobin adducts were characterized by high-resolution mass-spectrometry. Results showed that the species origins of individual myoglobins determined rates of non-enzymatic reduction (beef>equine>pork; P<0.05). Irrespective of species, pre-incubation of HNE myoglobin decreased non-enzymatic metmyoglobin reduction compared with control at both pH5.6 and 7.4 (P<0.05). Mass spectrometric analysis revealed adducts of HNE with bovine, porcine, and equine myoglobins. The results indicate that the amino acid composition and the covalent binding of HNE with myoglobin can significantly decrease the ability of heme to accept electrons.
•Non-enzymatic metmyoglobin reduction is species-specific.•Number of histidine residues determines non-enzymatic metmyoglobin reduction.•pH5.6 resulted in greater metmyoglobin reduction compared with pH7.4.•Covalent binding of HNE decreased metmyoglobin reduction.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>25828165</pmid><doi>10.1016/j.meatsci.2015.03.010</doi><tpages>6</tpages></addata></record> |
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| subjects | Aldehydes - pharmacology Animals Cattle Cross-Linking Reagents - pharmacology Dietary Proteins - chemistry Dietary Proteins - isolation & purification Dietary Proteins - metabolism Electron Transport - drug effects Horses Hydrogen-Ion Concentration Kinetics Lipid oxidation Lipid Peroxidation Mass spectrometry Meat color Metmyoglobin - chemistry Metmyoglobin - isolation & purification Metmyoglobin - metabolism Metmyoglobin reduction Models, Molecular Molecular Weight Myoglobin Oxidation-Reduction Pigments, Biological - chemistry Pigments, Biological - isolation & purification Pigments, Biological - metabolism Species Specificity Spectrometry, Mass, Electrospray Ionization Sus scrofa |
| title | Species-specific effects on non-enzymatic metmyoglobin reduction in vitro |
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