Two fragments from fibrinolysin digests of ovine prolactin: characterization and recombination to generate full immunoreactivity.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000941:Antigens; D001681:Biological Assay; D002942:Circular Dichroism; D005341:Fibrinolysin / Q000378:metabolism; D010446:Peptide Fragments / Q000276:immunology; D011388:Prolactin / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013552:Swine
D000596:Amino Acids; D000941:Antigens; D010446:Peptide Fragments; D011388:Prolactin; D005341:Fibrinolysin