J. Anim Sci.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Czerwinski, S. M.
Right arrow Articles by Martin, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Czerwinski, S. M.
Right arrow Articles by Martin, J. M.

Journal of Animal Science, Vol 72, Issue 5 1204-1208, Copyright © 1994 by American Society of Animal Science

JOURNAL ARTICLE

Effect of somatotropin on myosin expression in pigs

S. M. Czerwinski and J. M. Martin
U.S. Department of Agriculture, Beltsville, MD 20705.

Daily administration of recombinant porcine somatotropin (rpST) has marked effects on growth performance of swine. Protein accretion rates are dramatically increased with rpST treatment. However, the effect of rpST on specific muscle proteins has not been addressed. The purpose of this study was to examine the effects of rpST on 1) the distribution pattern of isomyosins, 2) the total myosin heavy chain protein levels, and 3) myosin heavy chain mRNA abundance present in swine skeletal muscle. There were no differences in myosin isoform composition in the longissimus muscle resulting from porcine somatotropin treatment. There were also no differences in the myosin heavy chain protein concentration within the longissimus muscles. In accordance with the protein levels, myosin heavy chain mRNA expression was not altered with rpST treatment. This study shows that although the pig responds to rpST with increased protein accretion rates, the proportion of myosin per milligram of total protein remains constant. Myosin was not altered by type, concentration, or expression level. By combining these tools we are now able to examine a myosin on both a protein and message level throughout growth.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1994 by the American Society of Animal Science.