Fischli, Walter and Goldstein, Avram and Hunkapiller, Michael W. and Hood, Leroy E. (1982) Isolation and amino acid sequence analysis of a 4,000-dalton dynorphin from porcine pituitary. Proceedings of the National Academy of Sciences of the United States of America, 79 (17). pp. 5435-5437. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:FISpnas82
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A 4,000-dalton dynorphin was isolated from porcine pituitary. It has 32 amino acids (Mr = 3,986), with the previously described heptadecapeptide (now called dynorphin A) at its amino terminus and a related tridecapeptide, dynorphin B, at its carboxyl terminus. The two peptides are separated by the "processing signal" Lys-Arg.
|Additional Information:||© 1982 by the National Academy of Sciences. Contributed by Avram Goldstein, June 17, 1982. We acknowledge the skilled technical assistance provided by Keiko Otsu and Patricia Lowery and the valuable participation of Louise I. Lowney at many stages of this investigation. The work was supported by grants from the National Institute on Drug Abuse (DA-1199 to A.G.), the Swiss National Foundation (to W.F.), the National Institutes of Health (GM-06965 to J. P. Revel), and the Weingart Foundation (to L.E.H.). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
|Subject Keywords:||opioid; peptide; endorphin; neuropeptide; prohormone|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||16 Mar 2007|
|Last Modified:||26 Dec 2012 09:33|
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