Isolation and identification of biologically active peptides
Following the discovery of some unidentified biologically active substance as a constituent of a living system, a full understanding of its role within that system must necessarily await its purification and the elucidation of a chemical structure. Without such detailed characteristisation we are limited to working with and observing the biological activity of a crude substance; this may lead to vague and speculative theories on interactions with other components in the system. Here, we are limiting our discussion to biologically active peptides, but unfortunately, because of the special factors discussed below, these are among the most difficult substances to evaluate structurally. For example, almost a decade of effort went into the structural determination of the hypothalamic hormone responsible for the release of thyroid stimulating hormone, despite the simplicity of the structure ultimately assigned to thyrotropin releasing hormone (TRH) (Burgus et al., 1969; Schally et al., 1966). Nevertheless, the work and the studies which this effort in turn stimulated has led to a revolution in our understanding of hypothalamic and pituitary function, and to a new appreciation of small peptides, not just as inactive fragments resulting from the enzymic digestion of proteins, but as a special class of compound exerting profound effects on the central nervous system.
KeywordsThyroid Stimulate Hormone Vasoactive Intestinal Peptide Thyrotropin Release Hormone Cyanogen Bromide Mass Spectrometric Method
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