Tipaporn LimpaseniMontri ChulavatnatolMahidol University2018-02-272018-02-271986-08-15Archives of Biochemistry and Biophysics. Vol.249, No.1 (1986), 154-16310960384000398612-s2.0-0022506643https://repository.li.mahidol.ac.th/handle/20.500.14594/9667An androgen-dependent sialoglycoprotein was purified from the secretion of rat ventral prostate by chromatofocusing and DEAE-Sepharose column chromatography. It showed a native molecular weight of 47,000 and consisted of two dissimilar subunits with molecular weights of 20,000 and 18,000. However, each subunit contained a common peptide with molecular weight of 16,000. It also contained 442 ± 62 μg sialic acids per milligram protein and bound pregnenolone with a binding affinity of 1.2 μm -1 . Its amino acid composition was similar to those of other known prostatic steroid-binding proteins. Hence, we propose that it is the sialylated form of rat prostatic steroid-binding protein. © 1986.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/0003-9861(86)90570-9