The structural features responsible for the high potency and opiate receptor specificity of the
opioid peptide dynorphin in the guinea pig ileum myenteric plexus were examined …

In the guinea-pig ileum myenteric plexus-longitudinal muscle preparation, products from the
dynorphin gene fell into three groups according to their potency. Dynorphin A was the most …

The full primary structure of the very potent opioid peptide dynorphin, from porcine pituitary,
has been determined. It is (H) Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp …

We describe the opioid properties of a tridecapeptide, the sequence of which corresponds to
the NH2-terminal sequence of dynorphin, a novel porcine pituitary endorphin. It contains …

The intrathecal delivery of dynorphin A (1-17) and (1-13) induces, with rapid onset, a severe
motor dysfunction characterized by flaccid extension of the hindlimbs and complete loss of …

Dynorphin A (dynA) and related opioid peptides produce moderate analgesic effects with
restricted types of pain stimuli that are often accompanied by a large variety of naloxone …

Dynorphin was recently isolated from porcine pituitary extracts and shown to be the most
potent known opioid peptide. Antisera were prepared to synthetic dynorphin-(1–13), the …

Like other opioids, the dynorphins play a role in wide variety of physiological parameters,
including pain regulation, motor activity, cardiovascular regulation, respiration, temperature …

The distribution of dynorphin in the central nervous system was investigated in rats
pretreated with relatively high doses (300–400 μg) of colchicine administered …

It is known that the opioid peptide dynorphin A has a broad distribution throughout the
neuraxis. Recent biochemical studies have extended the sequence of dynorphin A by 15 …