BioAcyl Corp |
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| Resource type: Journal Article DOI: https://doi.org/10.1016/0006-291X(81)91244-4 ID no. (ISBN etc.): 0006-291X BibTeX citation key: Kangawa1981 View all bibliographic details |
Categories: BioAcyl Corp Creators: Chino, Kangawa, Minamino Collection: Biochemical and Biophysical Research Communications |
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| Abstract |
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After re-purification by reverse phase high performance liquid chromatography, α-neo-endorphin was submitted to structural analyses, performed by dansyl-Edman degradation, as well as by C-terminal analysis by 3H-labeling. The full sequence of α-neo-endorphin has been determined to be : Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys, in which the 8th residue previously reported as Arg is found to be Tyr. A synthetic decapeptide with the above sequence was verified to be identical with natural α-neo-endorphin. For further structural confirmation, tryptic and chymotryptic peptides were also identified. Thus, the complete sequence of α-neo-endorphin has been definitely established. Its potent opioid activity in the guinea-pig ileum assay is also discussed.
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