PMID: 149984May 1, 1978Paper

Two fragments from fibrinolysin digests of ovine prolactin: characterization and recombination to generate full immunoreactivity

Proceedings of the National Academy of Sciences of the United States of America
Y Birk, C H Li

Abstract

The action of fibrinolysin (plasmin; EC 3.4.21.7) on ovine prolactin has been investigated. It was found that the enzyme selectively cleaves the bond between Met-53 and Ala-54. The two fragments, PRL-(1-53) and PRL-(54-199), have been purified and characterized. A recombinant molecule has been obtained by noncovalent interaction of PRL-(1-53) and PRL-(54-199). The recombined protein behaves nearly identically to the parent hormone in circular dichroism spectra and exclusion chromatography. The recombinant possesses full immunoreactivity, as revealed by gel double-diffusion and complement fixation. However, the recombined protein exhibits low prolactin activity in the pigeon crop-sac test.

References

May 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·C H Li, T A Bewley
Oct 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·C H LiA J Rao
Mar 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·C H LiT Hayashida
Feb 21, 1967·Biochimica Et Biophysica Acta·K R Woods, K T Wang

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Citations

Jan 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·T M WongC H Li
May 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·M D JibsonC B Glaser
Oct 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·B K ChoeN R Rose

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