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Titlebook: Glycoprotein Hormones; Structure, Function, Joyce W. Lustbader,David Puett,Raymond W. Ruddon Conference proceedings 1994 Springer-Verlag Ne

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Delineation of Subunit and Receptor Contact Sites by Site-Directed Mutagenesis of hCGβa species, the single α-subunit binds to distinct β-subunits to form bioactive holoproteins, which exhibit specificity for three G protein-coupled . (r) (2), LH/CGr (3), FSHr (4), and TSHr (5). Since the glycoprotein hormones contain a common α-subunit, and since both subunits are believed to partic
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https://doi.org/10.1007/978-3-322-87545-7re working on the purification of the glycoprotein hormones in the 1960s. There is little question that the isolation of highly purified gonadotropins (and thyrotropin) in the late 1950s and the 1960s, and the preparation of their subunits, provided a powerful stimulus to physiological and clinical
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Lehrbuch der Mathematischen Physiksful series published in . for the 75th anniversary of The Endocrine Society. I know one of my fellow honorees, Harold Papkoff, contributed a remembrance to that series (1) that I much admired, and I am sure he can do it again. The other fellow honoree, Robert J. Ryan, can always be counted on for t
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https://doi.org/10.1007/978-3-7091-6646-8distinct beta subunits that confer biological specificity (1). The common alpha subunit and each of the beta subunits are encoded by unique single copy genes that are expressed in specific cell types (gonadotropes: LH and FSH; thyrotropes: TSH) of the anterior pituitary gland (1, 2). LH and FSH are
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Analysis auf Mannigfaltigkeiten,es can occur at almost any point along the pathway from DNA to protein. The most common method that cells use to express specialized genes is to regulate the level of transcription of these genes (1). Combinations of transcription-enhancing and -repressing DNA binding factors can determine the level
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