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- W935251337 abstract "Publisher Summary Follicle stimulating hormone (FSH), luteinizing hormone (LH), human chorionic gonadotropin (hCG), and thyroid stimulating hormone (TSH) are glycoproteins, each composed of two dissimilar subunits, designated α and β. Those hormones contain a protein core with carbohydrate side chains that terminate in sialic acid or N-acetylneuramic acid, for the most part. A few side chains terminate in fucose. Selective enzymatic removal of sialic acid, known as “desialylation,” markedly reduces the in vivo biologic activity of hCG, FSH, and hLH. Studies performed with variably desialylated hCG preparations are consistent with a rapid disappearance of desialylated hormone from the plasma of rats, accounting for the reduced in vivo biologic activity of desialylated hCG. The immunologic behavior of highly purified hLH and urinary hFSH is altered with desialylation. The immunoreactivity of desialylated hLH and hFSH is significantly greater than that of the respective intact native hormone. On the other hand, the immunologic behavior of hCG is unaffected by desialylation. The two terminal exocyclic carbon atoms of sialic acid can be selectively removed chemically without destroying the ring structure of sialic acid or cleaving the glycosidic bonds present in glycoproteins." @default.
- W935251337 created "2016-06-24" @default.
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- W935251337 date "1975-01-01" @default.
- W935251337 modified "2023-10-17" @default.
- W935251337 title "[27] Tritium labeling of sialylated glycoprotein hormones" @default.
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- W935251337 doi "https://doi.org/10.1016/s0076-6879(75)37029-8" @default.
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