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- W82920908 abstract "During the past two decades, ß-endorphin's potent analgetic activity has stimulated intense research interest and the peptide has become ensconced in the popular imagination as the endogenous substance responsible for much that is deemed pleasurable in life. From a practical, analytical standpoint, ß-endorphin processing is important to consider because most of the antisera used to measure beta endorphin immunoreactivity recognize all six beta endorphin analogs as well as beta lipotropin. This methodological detail complicates the analysis of beta endorphin, in part because beta endorphin processing is tissue specific, which means that different tissues may synthesize completely different assortments of beta endorphin peptides yet, when measured by radioimmunoassay (RIA) contain equivalent amounts of beta endorphin immunoreactivity. This principle is clearly illustrated by beta endorphin processing in the anterior and intermediate lobes of the rat pituitary. This chapter reviews analytical methods commonly used to isolate ß-endorphin-related peptides from biological tissues, including plasma. In situ hybridization is based on the ability of relatively short sequences of DNA or RNA to penetrate into cells and hybridize with complementary regions of RNA or DNA in the cell. The ability to accurately estimate the amount of mRNA in the tissue is subject to a number of variables described in a protocol that is divided into three separate procedures that describe each component of the assay: preparation of the tissue, labeling of the probe, and hybridization of the probe specifically to the sequence of interest.." @default.
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- W82920908 date "1996-01-01" @default.
- W82920908 modified "2023-10-16" @default.
- W82920908 title "Chromatographic Methods for Analyzing β-Endorphin and Related Peptides" @default.
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- W82920908 doi "https://doi.org/10.1016/b978-012688460-9/50013-2" @default.
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