Ovine prolactin: equilibrium characteristics of the recombinant molecule formed by noncovalent interaction of two fibrinolysin fragments by fluorescence polarization.
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.
D000818:Animals; D002151:Calorimetry; D005341:Fibrinolysin / Q000378:metabolism*; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D007700:Kinetics; D008856:Microscopy, Fluorescence; D010446:Peptide Fragments / Q000032:analysis; D011388:Prolactin / Q000378:metabolism*; D011485:Protein Binding; D012756:Sheep; D013861:Thiocyanates
D005452:Fluoresceins; D010446:Peptide Fragments; D013861:Thiocyanates; D011388:Prolactin; D005341:Fibrinolysin; D016650:Fluorescein-5-isothiocyanate