Abstract
Following the structural elucidation of luteinizing hormone-releasing hormone (LH-RH) by Schally and associates, it became generally accepted that the decapeptide was a unique molecular form. This belief arose from:
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(a)
A number of studies purporting to have shown non-ribosomal biosynthesis of LH-RH and thereby excluding the possibility of ribosomally biosynthesised prohormonal forms.
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(b)
The assumption that LH-RH was confined to the CNS and thus unlikely to be present in other tissues in a modified form.
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(c)
Immunological and low resolution chromatographic studies demonstrating that LH-RH in the hypothalamus of nonmammalian vertebrates was identical to the mammalian peptide. This conclusion of a lack of interspecific differences in LH-RH structure in vertebrates was supported by the demonstration that synthetic mammalian LH-RH was biologically active in a wide range of mammalian species and in nonmammalian vertebrates (1).
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Millar, R.P., King, J.A. (1984). Molecular Heterogeneity of Luteinizing Hormone-Releasing Hormone. In: McKerns, K.W., Naor, Z. (eds) Hormonal Control of the Hypothalamo-Pituitary-Gonadal Axis. Biochemical Endocrinology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9960-5_30
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DOI: https://doi.org/10.1007/978-1-4684-9960-5_30
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