Abstract

The effect of gelatin (0·5 g/l) on binding curves at high dilution of three classes of stereo-specific binding proteins was studied. These included two antibodies (to oestradiol and aldosterone), six transins (horse and dog transcortins, human thyroxine-binding globulin, human sex steroid-binding globulin, and guinea pig transprogestin), and one receptor (bovine adrenal protein kinase). Gelatin increased the apparent binding of all these proteins, particularly at the highest dilutions and sometimes in a striking manner. While much of this action can be attributed to its decreasing the adhesion of the dilute binding protein to glass, gelatin also increased the apparent uptake of some tracers by certain adsorbents. Similar findings were obtained using human gamma globulin (2 g/l). These effects resulted in increased sensitivity and improved reproducibility in the assays employing them.