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|Title:||The Degradation Of Myofibrillar Proteins In Beef And Lamb Using Denaturing Electrophoresis: An Overview||Contributor(s):||Hopkins, D L (author); Thompson, John Mitchell (author)||Publication Date:||2002||DOI:||10.1111/j.1745-4573.2002.tb00323.x||Handle Link:||https://hdl.handle.net/1959.11/3921||Abstract:||Degradation of specific myofibrillar proteins has been followed in many studies using SDS-PAGE (denaturing) electrophoresis and these have shown that proteins such as titin, nebulin, troponin-T, desmin, filamin and vinculin are degraded at different rates during postmortem storage of meat. Although informative, electrophoresis is usually restricted to qualitative interpretation of the gels and there have been few studies that have quantitatively linked the degradation of specific proteins to changes in toughness. Improved quantitative methods (including scanning densitometry, image analysis, and modeling approaches) will be necessary to determine the protein and/or protein alterations that cause postmortem tenderization. This approach is complementary to other measurements of proteolysis where the objective is to more adequately explain the variation in toughness.||Publication Type:||Journal Article||Source of Publication:||Journal of Muscle Foods, 13(2), p. 81-102||Publisher:||Food & Nutrition Press Inc||Place of Publication:||Trumbull, CT, USA||ISSN:||1046-0756
|Field of Research (FOR):||070299 Animal Production not elsewhere classified||Socio-Economic Objective (SEO):||830301 Beef Cattle||Peer Reviewed:||Yes||HERDC Category Description:||C1 Refereed Article in a Scholarly Journal||Statistics to Oct 2018:||Visitors: 114
|Appears in Collections:||Journal Article|
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