The effects of iodination on the receptor binding affinity of ovine prolactin.
A completely iodinated form of ovine prolactin was prepared using lactoperoxidase. The iodination was characterized using gel filtration, electrophoresis and fluorescence analysis. Complete iodination corresponds to a 33% decrease in intrinsic tryptophanyl fluorescence (275 parallel 348). Each ovine prolactin molecule possesses four iodination sites which cannot be distinguished by kinetic analysis. The receptor binding capacity of the tetraiodoprolactin was also assayed using the particulate fraction from female rat livers. Although the total binding capacity of native and iodoprolactins is indistinguishable, significant differences in receptor binding behavior were observed.
D000818:Animals; D001667:Binding, Competitive; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes / Q000378:metabolism*; D011388:Prolactin / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011981:Receptors, Prolactin; D012756:Sheep; D013050:Spectrometry, Fluorescence
D007457:Iodine Radioisotopes; D011956:Receptors, Cell Surface; D011981:Receptors, Prolactin; D011388:Prolactin