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Title of article Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis

Grujić R., University of East Sarajevo , University of East Sarajevo

Savanović D., University of Banja Luka , University of Banja Luka

Year 2018 Issue 2 DOI 10.21603/2308-4057-2018-2-421-428
Annotation Myofibrillar and sarcoplasmic proteins were extracted from pork meat (M. Longissimus dorsi) and then separated by capillary gel electrophoresis (CGE). Migration time and peak areas of individual protein molecules in the electropherogram were analysed. The electropherograms obtained after the separation of myofibrillar proteins contained 53 well-separated peaks, of which the following were identified: thymosin, myosin light chain-3 (MLC-3), myosin light chain-2 (MLC-2), troponin C, troponin I, myosin light chain-1 (MLC-1), tropomyosin 1, tropomyosin 2, troponin T, actin, desmin, troponin, C protein, and myosin heavy chain (MHC). The relative concentration of the identified myofibrillar proteins was 74.5%. Of the 56 separated sarcoplasmic proteins the following were identified: myoglobin, myokinase, triosephosphate isomerase, phosphoglycerate mutase, lactate dehydrogenase, glyceraldehyde phosphate dehydrogenase, aldolase, creatine kinase, enolase, phosphoglucose isomerase, pyruvate kinase, phosphoglucomutase, and phosphorylase b. The relative concentration of the identified sarcoplasmic proteins was 83.6% of all sarcoplasmic proteins extracted from the pork meat.
Keywords Myofibrillar proteins, sarcoplasmic proteins, capillary gel electrophoresis
Artice information Received June 18, 2017
Accepted October 25, 2018
Available online December 20, 2018
Imprint article Grujić R. and Savanović D. Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis. Foods and Raw Materials, 2018, vol. 6, no. 2, pp. 421–428.
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