Abstract
The binding of androsterone sulfate, etiocholanolone sulfate and dehydroisoandrosterone sulfate to human serum, plasma and serum albumin was studied by equilibrium dialysis and ultrafiltration techniques. All 3 of these steroid sulfates are bound primarily to the albumin fraction of plasma. Androsterone sulfate and etiocholanolone sulfate are probably bound to the same 2 sets of sites on the albumin molecule with approximately the same force. Of the 2 sets of albumin sites for dehydroisoandrosterone sulfate, the set with greater binding affinity is different for this steroid than for the other 2. Characteristics of these binding sites for all 3 steroid sulfates are given.