Literature DB >> 17567165

Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period.

Xiaohong Jia1, Maria Ekman, Harald Grove, Ellen M Faergestad, Laila Aass, Kjell I Hildrum, Kristin Hollung.   

Abstract

Postmortem changes in protein composition up to 24 h in bovine longissimus thoracis muscle were investigated by two-dimensional gel electrophoresis and MALDI-TOF MS/MS. A total of 47 spots were significantly changed the first 24 h postmortem. The 39 identified proteins can be divided into five groups: metabolic enzymes, defense and stress proteins, structural proteins, proteolytic enzymes, and unclassified proteins. The identified metabolic enzymes are all associated with ATP-generating pathways, either the glycolytic pathway or energy metabolism. In addition, several defense and stress proteins were changed in abundance in this study. These findings contribute to a better understanding of the biochemical processes during postmortem storage of meat.

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Year:  2007        PMID: 17567165     DOI: 10.1021/pr070173o

Source DB:  PubMed          Journal:  J Proteome Res        ISSN: 1535-3893            Impact factor:   4.466


  11 in total

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Review 4.  Double Muscling in Cattle: Genes, Husbandry, Carcasses and Meat.

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Review 6.  Comparative Skeletal Muscle Proteomics Using Two-Dimensional Gel Electrophoresis.

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9.  Monitoring post mortem changes in porcine muscle through 2-D DIGE proteome analysis of Longissimus muscle exudate.

Authors:  Alessio Di Luca; Giuliano Elia; Anne Maria Mullen; Ruth M Hamill
Journal:  Proteome Sci       Date:  2013-03-20       Impact factor: 2.480

10.  Proteomic Changes in Sarcoplasmic and Myofibrillar Proteins Associated with Color Stability of Ovine Muscle during Post-Mortem Storage.

Authors:  Xiaoguang Gao; Dandan Zhao; Lin Wang; Yue Cui; Shijie Wang; Meng Lv; Fangbo Zang; Ruitong Dai
Journal:  Foods       Date:  2021-12-03
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