| Autor: |
Kilpatrick, D L, Taniguchi, T, Jones, B N, Stern, A S, Shively, J E, Hullihan, J, Kimura, S, Stein, S, Udenfriend, S |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; May 1981, Vol. 78 Issue: 5 p3265-3268, 4p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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