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Relaxin pp 315-322 | Cite as

Effect of a Purified Porcine Relaxin Upon Glycogen and Protein in the Rat Uterus

  • Edward H. Frieden
  • Peter VasilenkoIII
  • Walter C. Adams
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 143)

Abstract

The recent isolation (Sherwood and O’Byrne, 1974; Frieden et al., 1980) and characterization of porcine relaxin as a two-chain polypeptide bearing a distinct structural similarity to insulin (Schwabe and McDonald, 1977; James et al., 1977) has revived interest in an earlier report (Steinetz et al., 1950) that relaxin can exert glycogenic and protein anabolic effects in ovariectomized, estrogen- treated rats. Since the relaxins used in these early experiments were of relatively low specific activity (10–150 GPU/mg), we have examined the metabolic effects of purified, electrophoretically homogenous porcine relaxin as well as NIH-relaxin.

Keywords

Glycogen Content Uterine Weight Estradiol Benzoate Relaxin Receptor Blood Glucose Conc 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bray, G. A. (1960). A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Anal. Biochem. 1:279.CrossRefGoogle Scholar
  2. Demers, L. M., Yoshinaga and Greep, R. O. (1972). Uterine glycogen metabolism of the rat in early pregnancy. Biol. Reprod. 7: 297.CrossRefGoogle Scholar
  3. Frieden, E. H. and Hisaw, F. L. (1950). The purification of relaxin. Arch. Biochem. 29:166.PubMedGoogle Scholar
  4. Frieden, E. H., Rawitch, A. B., Wu, L. C. C. and Chen, S. W. C. (1980). The isolation of two proline-containing relaxin species from a porcine relaxin concentrate. Proc. Soc. Exp. Biol. Med. 163: 521.CrossRefGoogle Scholar
  5. James, R., Niall, H., Kwok, S. and Bryant-Greenwood, G. D. (1977). Primary structure of porcine relaxin: homology with insulin and related growth factors. Nature 267: 544.CrossRefGoogle Scholar
  6. McMurtry, J., Kwok, S. and Bryant-Greenwood, G. D. (1978). Target tissues for relaxin identified in vitro with 125I-labelled porcine relaxin. J. Reprod. Fertil. 53: 209.CrossRefGoogle Scholar
  7. Schwabe, C. and McDonald, J. K. (1977). Relaxin, a disulfide homolog of insulin. Science 197: 914.CrossRefGoogle Scholar
  8. Seifter, S., Dayton, S., Novie, B. and Muntwyler, E. (1950). Estimation of glycogen with the anthrone reagent. Arch. Biochem. 25:191.PubMedGoogle Scholar
  9. Sherwood, O. D., and O’Byrne, E. M. (1974). Purification and characterization of porcine relaxin. Arch. Biochem. Biophys. 160: 185.CrossRefGoogle Scholar
  10. Sherwood, O. D., and Crnekovic, V. E. (1979). Development of a homologous radioimmunoassay for rat relaxin. Proc. Soc. Exp. Biol. Med. 104:893.Google Scholar
  11. Steinetz, B. G, Beach, V. L., Blye, R. P. and Kroc, R. L. (1950). Changes in the composition of the rat uterus following a single injection of relaxin. Endocrinology 61: 166.Google Scholar
  12. Vasilenko, P., Ill, Frieden, E. H. and Adams, W. C. (1980). Effect of purified relaxin on uterine glycogen and protein in the rat. Proc. Soc. Exp. Biol. Med. 163: 245.CrossRefGoogle Scholar
  13. Walaas, O. (1952). Effect of estrogen on the glycogen content of the rat uterus. Acta Endocrinol. (Copenhagen). 10:175.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Edward H. Frieden
    • 1
  • Peter VasilenkoIII
    • 1
  • Walter C. Adams
    • 1
  1. 1.Departments of Chemistry and Biological SciencesKent State UniversityKentUSA

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