Abstract
A novel opioid analgesic peptide termed “Kyotorphin” was isolated and identified from bovine brain, using an in vivo analgesia assay method. The analgesic activity was assessed by a combination of intracisternal injection and the tail pinch test in mice. The sequence of this peptide was determined as Tyr-Arg by amino acid analysis and the N-terminal determination by the dansylation method. The natural peptide was confirmed to be identical to the synthetic peptide on TLC, HVPE and HPLC. The median analgesic dose, ED 50 of kyotorphin was 34.7 nmol/mouse with the tail pinch test and the potency was 4.2 times greater than that of met-enkephalin. With the hot plate test, the ED 50 of kyotorphin was 15.7 nmol/mouse and this effect was completely reversed by the pretreatment with naloxone (0.1 mg/kg, s.c.). The present analgesic assay method can thus be effectively applied to endogenous opioid substances to establish analgesic actions.
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