Abstract
A 3200-dalton adrenal enkephalin-containing peptide, designated peptide E, that exhibits high opiate activity in the guinea pig ileum longitudinal muscle preparation was purified, and its structure was determined. It contains an amino-terminal [Met]enkephalin sequence and a [Leu]enkephalin sequence at the carboxyl terminus. Sequence analysis revealed that peptide E arises from a previously characterized 4900-dalton adrenal enkephalin-containing peptide. Peptide E was shown to be 30 times more potent than [Met]enkephalin in the guinea pig ileum assay, which suggests that the adrenal enkephalin-containing peptide may perform a unique biological function in vivo.
MeSH Terms
Adrenal Medulla/analysis
Amino Acid Sequence
Animals
Biological Assay
Cattle
Cell Line
Chromaffin Granules/analysis
Chromaffin System/analysis
Endorphins/metabolism
Enkephalins/classification,metabolism
Glioma
Guinea Pigs
Ileum/drug effects
Mice
Molecular Weight
Muscle Contraction/drug effects
Neuroblastoma
Receptors, Opioid/metabolism
Chemicals
Endorphins
Enkephalins
Receptors, Opioid
adrenal opioid peptide E
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Kilpatrick D L
Taniguchi T
Jones B N
Stern A S
Shively J E
Hullihan J
Kimura S
Stein S
Udenfriend S
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