The synthesis of monkey (Macaca fascicularis) Sex steroid-Binding Protein (mSBP) in a wheat germ cell-free system in response to liver RNA was demonstrated by use of a specific antiserum raised against purified native human SBP. Antibodies precipitate a single translation product behaving as a 42 kDa protein in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Western blots of monkey sera subjected to SDS-PAGE and immunorevelation show that the native mSBP migrates as 2 molecular species (50 and 53 kDa) present in the approximate ratio of 1:10, respectively. The difference in apparent molecular weights of the primary translation product and the reduced mature mSBP may represent glycosylation that occurs post translationally. We describe for the first time the biosynthesis of mSBP at the molecular level and suggest that both components of mSBP derive from a common differentially processed precursor. Its mRNA is poorly represented, since the neosynthesized mSBP represents about 0.005% of the total proteins encoded by liver mRNA.