کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1192303 1492307 2011 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis
چکیده انگلیسی

Early postmortem changes of porcine muscle proteins including the rate and extent of pH decline, proteolysis and oxidation are key factors influencing the loss of water in meat, and proteolytic degradation may result in shrinking of muscle cells and drip loss. We report here the identification and structural characterisation of post-mortem degradation and oxidation of myofibrillar proteins using high resolution mass spectrometric proteomics. Soluble muscle proteins from M. Longissimus dorsi obtained 48 h postmortem at different drip loss were separated by two-dimensional gel electrophoresis (2D-PAGE), and degradation products were identified by Fourier-transform ion cyclotron resonance mass spectrometry. Oxidation products were detected by 2D-oxyblot analysis of 2,4-dinitrophenylhydrazine (DNPH)-treated proteins using an anti-DNP antibody, and selected spots were identified by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Postmortem denaturation at low drip loss was found for four contractile proteins, myosin-light chain-1; myosin regulatory light chain; α-β-tropomyosin and α-actin. The combination of 2D-PAGE and FTICR-MS was found to be a powerful approach for identification of muscle protein degradation products, providing identification of several truncation forms of creatine kinase and troponin T. The comparison of 2D-oxyblot and silver-stained 2D-gels at low and high drip loss revealed approximately 70 oxidatively modified proteins from muscle cell lysate. Oxidative modifications, representing possible biomarker candidates, were identified at Lys-170 of creatine kinase (4-hydroxynonenal), Lys-326 of actin (amino-adipic semialdehyde), and at W-169 (kynurenine) of triosephosphate isomerase.

Figure optionsDownload high-quality image (104 K)Download as PowerPoint slideResearch highlights▶ We report here the identification and structural characterisation of post-mortem degradation and oxidation of myofibrillar proteins using high resolution mass spectrometric proteomics. ▶ FTICR MS and tandem-MS provided the identification of oxidative modifications. ▶ The comparison of 2D-oxyblot and silver-stained 2D-gels at low and high drip loss revealed approximately 70 oxidatively modified proteins from muscle cell lysate. ▶ Oxidative modifications, representing possible biomarker candidates, were identified at Lys-170 of creatine kinase (4-hydroxynonenal), Lys-326 of actin (amino-adipic semialdehyde), and at W-169 (kynurenine) of triosephosphate isomerase.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Mass Spectrometry - Volume 305, Issues 2–3, 15 August 2011, Pages 217–227
نویسندگان
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