Purification and properties of an oestrogen-stimulated mouse uterine glycoprotein (approx. 70 kDa)

摘要: An oestrogen-induced secretory protein from mouse uterine luminal fluid was purified by CM-Affi-Gel Blue chromatography and reverse-phase h.p.l.c. This has an apparent molecular mass of approx. 70 kDa both SDS/polyacrylamide-gel electrophoresis (with or without 2-mercaptoethanol) gel-filtration column chromatography, indicating that it exists as a single-chain polypeptide. Further analysis the revealed is highly basic (pI greater than equal to 10) glycoprotein. The N-terminus appears be blocked Edman degradation. partial amino acid sequence fragment obtained cleavage with CNBr; no homology between analysed other known sequences. incorporation [35S]methionine into proteins in vitro oestrogen treatment immature mice stimulates synthesis secretion protein. enzyme-linked immunosorbent assay polyclonal antibody used determine tissue distribution Tissues such lung, brain, spleen, muscle, intestine, liver, kidney ovary oestrogen-treated did not have detectable amounts Immunoreactivity present vaginal tissues animals. induced testosterone progesterone. Although function this unknown, useful marker for study action mammalian uterus well regulation gene expression at level.