Abstract
Endorphin has been isolated from an acid acetone extract of the pituitary of the salmon Oncorhynchus keta by ion exchange chromatography and gel filtration. Sequence analysis revealed it to be a nonacosapeptide with following primary structure: Ac-Tyr-Gly-Gly-Phe-Met-Lys-Pro-Tyr-Thr-Lys-Gln-Ser-His-Lys-Pro-Leu-Ile-Thr-Leu-Leu-Lys-His- Ile-Thr-Leu-Lys-Asn-Glu-Gln-OH. It appears that the amino terminal segment which is necessary for analgesic activity is conserved through the evolution of vertebrate except for the blocking of the amino terminal of salmon endorphin.
Original language | English |
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Pages (from-to) | 1249-1254 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 88 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1979 Jun 27 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology