Abstract
Four beta-endorphin-like peptides from bovine brain extracts have been identified by their behavior in CM-cellulose chromatography, gel filtration, high-performance liquid chromatography, and radioimmunoassay. Two of them have been isolated in sufficient quantity for amino acid analysis, radioimmunoassay, and radioreceptor assay. One peptide has an amino acid composition nearly identical to that of beta-endorphin with 56% of the radioimmunoreactivity and 2.3% of the potency in the radioreceptor assay of beta-endorphin. The amino acid content of the other beta-endorphin-like peptide is very different from that of bovine beta-endorphin but it has 47% of the radioimmunoreactivity and 1% of the potency in the radioreceptor assay of beta-endorphin.
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Selected References
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