Isolation and amino acid sequence analysis of a 4,000-dalton dynorphin from porcine pituitary.
- 1 September 1982
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 79 (17) , 5435-5437
- https://doi.org/10.1073/pnas.79.17.5435
Abstract
A 4000-dalton dynorphin was isolated from porcine pituitary. It has 32 amino acids (MW = 3986), with the previously described heptadecapeptide (now called dynorphin A) at its amino terminus and a related tridecapeptide, dynorphin B, at its carboxyl terminus. The 2 peptides are separated by the processing signal Lys-Arg.This publication has 21 references indexed in Scilit:
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