Gonadotropic Hormones by Choh Hao Li

By Choh Hao Li

Hormonal Proteins and Peptides, quantity XI: Gonadotropic Hormones offers with gonad stimulating hormones that reason precocious sexual maturity.

This publication starts off by means of reviewing the connection of the chemical constitution to the organic job of gonadotropins and chorionic hormones, by way of a short presentation at the in vitro bioassay tools. A finished dialogue on a few features of the molecular mechanism of gonadotropin motion is additionally supplied. This book concludes with an research of the immunobiology of gonadotropins.

This publication is meant for endocirnologists, yet can be worthy for clinical practitioners and researchers concerned about gonadotropic hormones.

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The subunit can only be reduced fully when it is denaturated, and the modified subunit cannot be refolded into the native confor­ mation, perhaps because of disulfide interchanges that occur when more than two cystines are reduced (Reeve and Pierce, 1981). Even partially reduced LH β with a single disulfide opened cannot reoxidize and recombine with the native β subunit (Reeve and Pierce, 1981). Such inter­ changes, which may occur during the preparation of subunits in lengthy procedures, may be responsible for the failures to generate full activity during recombination (Reeve and Pierce, 1981).

The sequence of hTSH β is from Sairam and Li (1977). For other references see Table I and Pierce and Parsons (1981). unusual features in the proposed determinant (loop region) that could explain their anomalous behavior. It is possible that there are other do­ mains in the three dimensional structures, some overlap of which could induce hormonal cross-reactivity. Further studies directed at examining the differential effects of modifi­ cation on the activity of these similar hormones with emphasis on quanti­ tative assessment may reveal the underlying basis of the specificity of hormone receptor interactions.

Much of the data on structure-function relationships have come from studies on ovine and bovine LH, hCG, and bovine TSH. Similar studies on FSH are made difficult by the inavailability of this hormone in sufficient quantity. A . AMINO GROUPS The subunits of LH and FSH from most species contain free a amino and ε amino groups, with two exceptions. , 22 M. R. SAIRAM 1973) (see Fig. 3). Its a amino group is also reported to be blocked. That such a β subunit can give rise to a biologically active hormone indicates that the presence of a positively charged amino group at corresponding positions is not essential for subunit recognition nor for binding to re­ ceptor.

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