Purification and characterization of the sex steroid binding protein from macaque serum. Comparison with the human protein.

The sex steroid binding protein (SBP) of Macaca mulatta and Macaca nemestrina sera has been purified to homogeneity and chemically characterized. The native protein is a glycoprotein having a molecular weight of approximately 88 000 and is composed of two similar subunits of molecular weight 47 000 as estimated by sodium dodecyl sulfate gel electrophoresis. One molecule of 5 alpha-dihydrotestosterone is bound per dimer with a KD equal to 1.6 nM at 11 degrees C. Isoelectric focusing patterns reveal the presence of at least 12 different forms of dimeric SBP molecules probably resulting from the presence of different amounts or types of carbohydrate side chains. The data indicate a very close similarity in molecular and steroid-binding properties to human SBP and establish the macaque monkey as a valuable animal model to study the physiological role of SBP in humans.