Please use this identifier to cite or link to this item: https://hdl.handle.net/1959.11/3921
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
1745-4573
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
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