Purification and characterization of a steroid-binding sialoglycoprotein from rat ventral prostate.
An 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 micrograms sialic acids per milligram protein and bound pregnenolone with a binding affinity of 1.2 microM-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.
D000596:Amino Acids / Q000032:analysis; D000727:Androgen-Binding Protein / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002850:Chromatography, Gel; D007526:Isoelectric Point; D008297:Male; D008970:Molecular Weight; D011284:Pregnenolone / Q000378:metabolism; D011467:Prostate / Q000032:analysis* / Q000378:metabolism; D060789:Prostatein; D051381:Rats; D060765:Secretoglobins; D012795:Sialoglycoproteins / Q000302:isolation & purification* / Q000378:metabolism; D014598:Uteroglobin; D060788:Mammaglobin B
D000596:Amino Acids; D000727:Androgen-Binding Protein; D011284:Pregnenolone; D060789:Prostatein; D060765:Secretoglobins; D012795:Sialoglycoproteins; D014598:Uteroglobin; C511484:Scgb1d2 protein, rat; C511483:Scgb1d4 protein, rat; C556468:Scgb2a1 protein, rat; D060788:Mammaglobin B