Ractopamine-induced changes in sarcoplasmic proteome profile of post-rigor pork semimembranosus muscle

J. Wu, M. N. Nair, S. P. Suman, S. Li, X. Luo, C. M. Beach, B. M. Bohrer, D. D. Boler

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Ractopamine is a beta-adrenergic agonist that increases leanness and carcass weight in finishing pigs. Our previous study observed that dietary ractopamine increased the abundance of several glycolytic enzymes in the sarcoplasmic proteome of post-rigor pork longissimus thoracis muscle. Pork semimembranosus is an economically important muscle and demonstrates differences in biochemistry compared with longissimus thoracis. Nonetheless, the effects of ractopamine on sarcoplasmic proteome of semimembranosus have not been evaluated yet. Therefore, this study examined the influence of ractopamine on sarcoplasmic proteome of post-rigor pork semimembranosus. Analyses of sarcoplasmic proteome of semimembranosus muscles from control (CON; diet without ractopamine) and ractopamine-fed (RAC; 7.4 mg/kg for 14 days followed by 10.0 mg/kg for 14 days) barrows revealed that haemoglobin subunit beta, alpha-crystallin B, and titin fragments were over-abundant in CON. In contrast, myosin light chain 1/3 and tripartite motif-containing protein 72 were over-abundant in RAC. The low abundance of haemoglobin subunit beta and alpha crystallin B in RAC could be attributed to fibre type shift (from oxidative to glycolytic) in response to ractopamine. The over-abundance of MLC 1/3 and tripartite motif-containing protein 72 in RAC could be due to the increased myofibrillar protein synthesis and muscle mass in ractopamine-fed pigs. Dietary ractopamine decreased the abundance of sarcoplasmic proteins involved in oxygen transport and chaperone activity, but increased the abundance of proteins involved in muscle contraction and plasma membrane repair in pork semimembranosus muscle.

Original languageEnglish
Pages (from-to)640-647
Number of pages8
JournalSouth African Journal of Animal Sciences
Issue number5
StatePublished - 2017

Bibliographical note

Funding Information:
This is publication number 17-07-049 of the Kentucky Agricultural Experiment Station and is published with the approval of the director. This work is supported by the National Institute of Food and Agriculture, U.S. Department of Agriculture, Hatch-Multistate Project 1008755. Mass spectrometric analysis was performed at the University of Kentucky’s Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research.


  • Pork
  • Ractopamine
  • Sarcoplasmic proteome
  • Semimembranosus

ASJC Scopus subject areas

  • Animal Science and Zoology


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