ICAR Research Data Repository for Knowledge Management
Species-specific myoglobin oxidation.
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View Archive Info| Field | Value | |
| Title |
Species-specific myoglobin oxidation.
Not Available |
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| Creator |
Shuang Y, Faustman C, Tatiyaborworntham N, Ramanathan R, Maheswarappa Naveena, Mancini R, Joseph P, Suman S.P and Sun Q
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| Subject |
Species specific Myoglobin oxidation
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| Description |
Not Available
The effect of the lipid oxidation product, 4-hydroxy-2-nonenal (HNE), on oxidation of oxymyoglobin (OxyMb) from seven different meat-producing species was investigated. Relative to controls, HNE increased OxyMb oxidation within all species (p < 0.05) at both 25 and 4 °C, pH 5.6. The relative effect of HNE was greater for myoglobins (Mbs) that contained 12 ± 1 histidine (His) residues than for those that contained 9 His residues (p < 0.05); HNE efficacy in all species except chicken and turkey decreased with time. Mono-HNE adducts were detected in all species except chicken and turkey. In general, HNE alkylation increased the Mbs' ability to accelerate lipid oxidation in a microsome model. However, neither an HNE nor a Mb species dependent effect was observed. Results suggested that microsome model system associated lipid oxidation overshadowed HNE and species effects on OxyMb oxidation observed in lipid-free systems. Not Available |
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| Date |
2018-09-22T06:31:15Z
2018-09-22T06:31:15Z 2011-12-31 |
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| Type |
Article
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| Identifier |
Not Available
Not Available http://krishi.icar.gov.in/jspui/handle/123456789/7146 |
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| Language |
English
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| Relation |
Not Available;
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| Publisher |
ACS Publications
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