Open AccessOvine prolactin: equilibrium characteristics of the recombinant molecule formed by noncovalent interaction of two fibrinolysin fragments by fluorescence polarization.
Author(s) -
Michael D. Jibson,
Choh Hao Li,
Charles L. Glaser
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.5.2830
Subject(s) - chemistry , fluorescence anisotropy , fluorescence , diazirine , dissociation constant , dissociation (chemistry) , molecule , recombinant dna , covalent bond , prolactin , biophysics , stereochemistry , biochemistry , biology , hormone , organic chemistry , physics , receptor , quantum mechanics , membrane , gene
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.