Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. I. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones.

摘要: We have elucidated the structures of anionic asparagine-linked oligosaccharides present on glycoprotein hormones lutropin (luteinizing hormone), follitropin (follicle-stimulating and thyrotropin (thyroid-stimulating hormone). Purified hormones, isolated from bovine, ovine, human pituitaries, were digested with N-glycanase, released reduced NaB[3H]4. The 3H-labeled each hormone then fractionated by anion-exchange high performance liquid chromatography (HPLC) into populations differing in number sulfate and/or sialic acid moieties. further purified as well structurally characterized using a variety preparative analytical techniques, including HPLC, endo- exoglycosidase digestions, lectin affinity chromatography. sulfated, sialylated, sulfated/sialylated structures, which together comprised 67-90% pituitary highly heterogeneous displayed hormone- animal species-specific features. sulfated consisted hybrid complex type one or two branches terminating SO4-4GalNAc beta 1,4. In contrast, sialylated wide array containing three peripheral one, two, A previously uncharacterized dibranched oligosaccharide, bearing residue acid, was found all except bovine lutropin. this study, we describe purification detailed structural characterizations lutropin, follitropin, several species. accompanying paper (Green, E.D., Baenziger, J.U.(1987) J. Biol. Chem. 262, 36-44) demonstrate marked quantitative differences among terms sulfation, sialylation, underlying oligosaccharide provide evidence for site-specific synthesis individual hormones.