文章基本信息

标题：Isolation and amino acid sequence analysis of a 4,000-dalton dynorphin from porcine pituitary
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作者：W Fischli ; A Goldstein ; M W Hunkapiller 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1982
卷号：79
期号：17
页码：5435-5437
DOI：10.1073/pnas.79.17.5435
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.