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. 1981 May;78(5):2830–2832. doi: 10.1073/pnas.78.5.2830

Ovine prolactin: equilibrium characteristics of the recombinant molecule formed by noncovalent interaction of two fibrinolysin fragments by fluorescence polarization.

M D Jibson, C H Li, C B Glaser
PMCID: PMC319451  PMID: 6454891

Abstract

The equilibrium characteristics of the recombined molecule formed by noncovalent interaction of two fibrinolysin fragments of ovine prolactin (oPRL) have been studied with fluorescence polarization. Fluorescein isothiocyanate (isomer I) was used to label oPRL-(1-53), creating a fluorescent peptide indistinguishable from the unlabeled fragment in the complementation reaction with oPRL-(54-199). The dissociation constant of the recombinant prolactin was 0.144 microM at 30 degrees C, with a free energy of dissociation of 9.50 kcal/mol.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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